ID V5VCW7_ACIBA Unreviewed; 275 AA. AC V5VCW7; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 26-FEB-2020, entry version 66. DE RecName: Full=Methionine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653}; DE Short=MAP {ECO:0000256|HAMAP-Rule:MF_01974}; DE Short=MetAP {ECO:0000256|HAMAP-Rule:MF_01974}; DE EC=3.4.11.18 {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653}; DE AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_01974}; GN Name=map {ECO:0000256|HAMAP-Rule:MF_01974, GN ECO:0000313|EMBL:PZM18289.1}; GN Synonyms=map1 {ECO:0000313|EMBL:AKA30982.1}, map_1 GN {ECO:0000313|EMBL:KZA22651.1}, map_2 {ECO:0000313|EMBL:ASF78035.1}; GN ORFNames=A7M79_08180 {ECO:0000313|EMBL:OIH08354.1}, A7M90_04815 GN {ECO:0000313|EMBL:OIG72371.1}, ABUW_1234 GN {ECO:0000313|EMBL:AKA30982.1}, B4R90_02870 GN {ECO:0000313|EMBL:OVL12321.1}, B9X91_03550 GN {ECO:0000313|EMBL:OTL50035.1}, B9X95_11705 GN {ECO:0000313|EMBL:OTM85450.1}, BGC29_02575 GN {ECO:0000313|EMBL:ODP71121.1}, C2U32_08280 GN {ECO:0000313|EMBL:AUT38008.1}, CBI29_02666 GN {ECO:0000313|EMBL:ASF78035.1}, CHQ89_03925 GN {ECO:0000313|EMBL:OZT31344.1}, CPI82_15740 GN {ECO:0000313|EMBL:PHQ01666.1}, CSB70_2491 GN {ECO:0000313|EMBL:AVI33300.1}, DOL94_04640 GN {ECO:0000313|EMBL:PZM18289.1}, E2533_16370 GN {ECO:0000313|EMBL:TEX13795.1}, E2536_05045 GN {ECO:0000313|EMBL:TEX30240.1}, E5294_06205 GN {ECO:0000313|EMBL:TGZ07088.1}, E5979_19040 GN {ECO:0000313|EMBL:TGY98765.1}, EA685_09240 GN {ECO:0000313|EMBL:RSR10093.1}, EA706_00955 GN {ECO:0000313|EMBL:RSQ49839.1}, EA722_08630 GN {ECO:0000313|EMBL:RSP76616.1}, EA746_001715 GN {ECO:0000313|EMBL:THJ60216.1}, EKS29_06595 GN {ECO:0000313|EMBL:RTY10994.1}, EWO92_05210 GN {ECO:0000313|EMBL:RYL18680.1}, EWO96_05210 GN {ECO:0000313|EMBL:RYL31564.1}, EWP49_05205 GN {ECO:0000313|EMBL:RYL46242.1}, FD887_09880 GN {ECO:0000313|EMBL:TLT63582.1}, FD913_06295 GN {ECO:0000313|EMBL:TLT67225.1}, FJU36_01850 GN {ECO:0000313|EMBL:TPU81270.1}, FJU42_15260 GN {ECO:0000313|EMBL:TPU61657.1}, FJU76_01715 GN {ECO:0000313|EMBL:TPS97919.1}, FJU79_05820 GN {ECO:0000313|EMBL:TPS87062.1}, FJU87_03675 GN {ECO:0000313|EMBL:TPU23229.1}, FJV14_00180 GN {ECO:0000313|EMBL:TPS05618.1}, FQK04_05410 GN {ECO:0000313|EMBL:TWO50388.1}, LV38_03303 GN {ECO:0000313|EMBL:KZA22651.1}, NCTC13305_03581 GN {ECO:0000313|EMBL:SUU32078.1}, SAMEA104305283_01206 GN {ECO:0000313|EMBL:SSS24419.1}, SAMEA104305318_02021 GN {ECO:0000313|EMBL:SST23566.1}, SAMEA104305351_02247 GN {ECO:0000313|EMBL:SSU74255.1}; OS Acinetobacter baumannii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=470 {ECO:0000313|EMBL:PZM18289.1, ECO:0000313|Proteomes:UP000248662}; RN [1] {ECO:0000313|EMBL:AKA30982.1, ECO:0000313|Proteomes:UP000032746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB5075-UW {ECO:0000313|EMBL:AKA30982.1, RC ECO:0000313|Proteomes:UP000032746}; RX PubMed=25845845; RA Gallagher L.A., Ramage E., Weiss E.J., Radey M., Hayden H.S., Held K.G., RA Huse H.K., Zurawski D.V., Brittnacher M.J., Manoil C.; RT "Resources for Genetic and Genomic Analysis of Emerging Pathogen RT Acinetobacter baumannii."; RL J. Bacteriol. 197:2027-2035(2015). RN [2] {ECO:0000313|Proteomes:UP000032746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB5075-UW {ECO:0000313|Proteomes:UP000032746}; RA Gallagher L.A., Hayden H.S., Weiss E.J., Hager K.R., Ramage E., Radey M.R., RA Bydalek R., Manoil C., Miller S.I., Brittnacher M.J.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:KZA22651.1, ECO:0000313|Proteomes:UP000076314} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB3638 {ECO:0000313|EMBL:KZA22651.1, RC ECO:0000313|Proteomes:UP000076314}; RA Arivett B.A., Fiester S.E., Ream D.C., Actis L.A.; RT "Draft sequences of Acinetobacter baumannii isolates from wounded military RT personnel."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:OIG72371.1, ECO:0000313|Proteomes:UP000179791, ECO:0000313|Proteomes:UP000179937} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XH639 {ECO:0000313|EMBL:OIH08354.1, RC ECO:0000313|Proteomes:UP000179791}, and XH647 RC {ECO:0000313|EMBL:OIG72371.1, ECO:0000313|Proteomes:UP000179937}; RA Hua X., Yu Y.; RT "The evolution of Acinetobacter baumannii in vivo."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:ODP71121.1, ECO:0000313|Proteomes:UP000094982} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XH198 {ECO:0000313|EMBL:ODP71121.1, RC ECO:0000313|Proteomes:UP000094982}; RA Mu X., Wang N., Li X., Shi K., Zhou Z., Yu Y., Hua X.; RT "The effect of colistin resistance-associated mutations on the fitness of RT Acinetobacter baumannii."; RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:OVL12321.1, ECO:0000313|Proteomes:UP000195460} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABUH557 {ECO:0000313|EMBL:OVL12321.1, RC ECO:0000313|Proteomes:UP000195460}; RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I., RA Dimitrov K.M., Suarez D.L., Swayne D.E.; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:OTL50035.1, ECO:0000313|Proteomes:UP000194699, ECO:0000313|Proteomes:UP000194957} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR350 {ECO:0000313|EMBL:OTM85450.1, RC ECO:0000313|Proteomes:UP000194699}, and PR354 RC {ECO:0000313|EMBL:OTL50035.1, ECO:0000313|Proteomes:UP000194957}; RA Song R., Chenine A.L., Ruprecht R.M.; RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:ASF78035.1, ECO:0000313|Proteomes:UP000197701} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A85 {ECO:0000313|EMBL:ASF78035.1, RC ECO:0000313|Proteomes:UP000197701}; RA Hamidian M., Wick R.R., Hawkey J., Holt K.E., Hall R.M.; RT "Complete genome sequence of Acinetobacter baumannii strain A85 belonging RT to global clone 1 (GC1)."; RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:OZT31344.1, ECO:0000313|Proteomes:UP000216874} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DR1 {ECO:0000313|EMBL:OZT31344.1, RC ECO:0000313|Proteomes:UP000216874}; RA Srinivasan V.B., Rajamohan G.; RT "Genome sequence, assembly and annotation."; RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:PHQ01666.1, ECO:0000313|Proteomes:UP000223291} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=I43 {ECO:0000313|EMBL:PHQ01666.1, RC ECO:0000313|Proteomes:UP000223291}; RA Siqueira K.A., Mello I.S., Mendes T.A., Soares M.A.; RT "Draft genome of Acinetobacter baumannii strain I43, a mercury resistant RT bacteria."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|Proteomes:UP000236385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABNIH28 {ECO:0000313|Proteomes:UP000236385}; RX PubMed=29437920; RG NISC Comparative Sequencing Program; RA Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P., RA Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J., RA Henderson D.K., Palmore T.N., Segre J.A., Frank K.M.; RT "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of RT Bacterial Plasmids Conferring Carbapenem Resistance."; RL MBio 9:e02011-17(2018). RN [12] {ECO:0000313|EMBL:AUT38008.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABNIH28 {ECO:0000313|EMBL:AUT38008.1}; RG NISC Comparative Sequencing Program; RA Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P., RA Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J., RA Henderson D.K., Palmore T.N., Segre J.A., Frank K.M.; RT "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of RT Bacterial Plasmids Conferring Carbapenem Resistance."; RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases. RN [13] {ECO:0000313|EMBL:AUT38008.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABNIH28 {ECO:0000313|EMBL:AUT38008.1}; RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.; RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases. RN [14] {ECO:0000313|Proteomes:UP000236385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABNIH28 {ECO:0000313|Proteomes:UP000236385}; RA Segre J.A., Mullikin J.; RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases. RN [15] {ECO:0000313|EMBL:AVI33300.1, ECO:0000313|Proteomes:UP000257523} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AR_0070 {ECO:0000313|EMBL:AVI33300.1, RC ECO:0000313|Proteomes:UP000257523}; RA Benahmed F.H., Lutgring J.D., Yoo B., Machado M., Brown A., McAllister G., RA Perry A., Halpin A.L., Vavikolanu K., Ott S., Zhao X., Tallon L., RA Sadzewicz L., Aluvathingal J., Nadendla S., Voskania-kordi A., Simonyan V., RA Patel J., Shawar R.M.; RT "FDA/CDC Antimicrobial Resistant Isolate Bank Genome Sequencing."; RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases. RN [16] {ECO:0000313|EMBL:PZM18289.1, ECO:0000313|Proteomes:UP000248662} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R10 {ECO:0000313|EMBL:PZM18289.1, RC ECO:0000313|Proteomes:UP000248662}; RA Bonnin R.A., Levy M., Cuzon G., Dortet L., Naas T.; RT "Carbapenemase-producing Acinetobacter spp. from environmental sources in RT an hospital from French Polynesia."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [17] {ECO:0000313|EMBL:SUU32078.1, ECO:0000313|Proteomes:UP000255154} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC13305 {ECO:0000313|EMBL:SUU32078.1, RC ECO:0000313|Proteomes:UP000255154}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [18] {ECO:0000313|Proteomes:UP000252694, ECO:0000313|Proteomes:UP000253591, ECO:0000313|Proteomes:UP000264160} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4300STDY7045788 {ECO:0000313|EMBL:SSS24419.1, RC ECO:0000313|Proteomes:UP000264160}, 4300STDY7045823 RC {ECO:0000313|EMBL:SST23566.1, ECO:0000313|Proteomes:UP000252694}, and RC 4300STDY7045856 {ECO:0000313|EMBL:SSU74255.1, RC ECO:0000313|Proteomes:UP000253591}; RG Pathogen Informatics; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [19] {ECO:0000213|PDB:6MRF} RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 12-272. RA Edwards T.E., Mayclin S.J., Lorimer D.D., Horanyi P.S., RA Seattle Structural Genomics Center for Infectious Disease.; RT "Crystal structure of a Methionine aminopeptidase MetAP from Acinetobacter RT baumannii."; RL Submitted (OCT-2018) to the PDB data bank. RN [20] {ECO:0000313|Proteomes:UP000269597, ECO:0000313|Proteomes:UP000271711, ECO:0000313|Proteomes:UP000272401} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TG22168 {ECO:0000313|EMBL:RSQ49839.1, RC ECO:0000313|Proteomes:UP000272401}, TG31299 RC {ECO:0000313|EMBL:RSP76616.1, ECO:0000313|Proteomes:UP000269597}, RC TG31307 {ECO:0000313|Proteomes:UP000280982}, and TG41016 RC {ECO:0000313|EMBL:RSR10093.1, ECO:0000313|Proteomes:UP000271711}; RA Sahl J.W.; RT "GWAS and RNA-Seq identify cryptic mechanisms of antimicrobial resistance RT in Acinetobacter baumannii."; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. RN [21] {ECO:0000313|EMBL:THJ60216.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TG31307 {ECO:0000313|EMBL:THJ60216.1}; RA Sahl J.W.; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. RN [22] {ECO:0000313|EMBL:RTY10994.1, ECO:0000313|Proteomes:UP000278858} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM107 {ECO:0000313|EMBL:RTY10994.1, RC ECO:0000313|Proteomes:UP000278858}; RA Fouts D.E., Sutton G., Singh I., Nguyen K.; RT "Na."; RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases. RN [23] {ECO:0000313|Proteomes:UP000291489, ECO:0000313|Proteomes:UP000292081, ECO:0000313|Proteomes:UP000292122} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C1T1-1 {ECO:0000313|EMBL:RYL46242.1, RC ECO:0000313|Proteomes:UP000291489}, C1T1-2_b RC {ECO:0000313|EMBL:RYL31564.1, ECO:0000313|Proteomes:UP000292081}, and RC C1T1-3 {ECO:0000313|EMBL:RYL18680.1, RC ECO:0000313|Proteomes:UP000292122}; RA Rehman M.A.; RT "Whole-Genome Sequences of Acinetobacter spp Isolated From Dairy Cow RT Manure."; RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases. RN [24] {ECO:0000313|EMBL:TEX13795.1, ECO:0000313|Proteomes:UP000297480, ECO:0000313|Proteomes:UP000297782} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MDR-CQB {ECO:0000313|EMBL:TEX13795.1, RC ECO:0000313|Proteomes:UP000297782}, and MDR-CQE RC {ECO:0000313|EMBL:TEX30240.1, ECO:0000313|Proteomes:UP000297480}; RA Jian Z.; RT "Resequencing Analysis and Multi-drug Resistance Differences of RT Acinetobacter baumannii in Chongqing, China."; RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases. RN [25] {ECO:0000313|EMBL:TGZ07088.1, ECO:0000313|Proteomes:UP000307835} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DMC-32a {ECO:0000313|EMBL:TGZ07088.1, RC ECO:0000313|Proteomes:UP000307835}; RA Jahan M.I., Hossain M.A., Sultana M.; RT "Complete genome of Acinetobacter baumannii."; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. RN [26] {ECO:0000313|EMBL:TGY98765.1, ECO:0000313|Proteomes:UP000310129} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ab5038 {ECO:0000313|EMBL:TGY98765.1, RC ECO:0000313|Proteomes:UP000310129}; RA Grana-Miraglia L., Castillo-Ramirez S., Cevallos M.A.; RT "Genome diversity A. baumannii Mexican isolates."; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. RN [27] {ECO:0000313|EMBL:THJ60216.1, ECO:0000313|Proteomes:UP000280982} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TG31307 {ECO:0000313|EMBL:THJ60216.1, RC ECO:0000313|Proteomes:UP000280982}; RA Sahl J.; RT "Genome wide association studies (GWAS) and transcriptomics identifies RT cryptic antimicrobial resistance mechanisms in Acinetobacter baumannii."; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. RN [28] {ECO:0000313|EMBL:TLT63582.1, ECO:0000313|Proteomes:UP000306363, ECO:0000313|Proteomes:UP000309525} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Aci00849 {ECO:0000313|EMBL:TLT67225.1, RC ECO:0000313|Proteomes:UP000309525}, and Aci00859 RC {ECO:0000313|EMBL:TLT63582.1, ECO:0000313|Proteomes:UP000306363}; RA Eigenbrod T., Reuter S., Gross A., Kocer K., Guenther F., Zimmermann S., RA Heeg K., Mutters N.T., Nurjadi D.; RT "Molecular characterization of carbapenem-resistant Acinetobacter baumannii RT using whole-genome sequencing revealed missed transmission events, Germany, RT 2012-2015."; RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases. RN [29] {ECO:0000313|Proteomes:UP000315888, ECO:0000313|Proteomes:UP000318271, ECO:0000313|Proteomes:UP000318526} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MRSN14237 {ECO:0000313|EMBL:TPU61657.1, RC ECO:0000313|Proteomes:UP000315888}, MRSN14427 RC {ECO:0000313|EMBL:TPU81270.1, ECO:0000313|Proteomes:UP000320149}, RC MRSN22112 {ECO:0000313|EMBL:TPU23229.1, RC ECO:0000313|Proteomes:UP000318586}, MRSN32875 RC {ECO:0000313|EMBL:TPS97919.1, ECO:0000313|Proteomes:UP000318271}, RC MRSN337038 {ECO:0000313|EMBL:TPS87062.1, RC ECO:0000313|Proteomes:UP000318526}, and MRSN7460 RC {ECO:0000313|EMBL:TPS05618.1, ECO:0000313|Proteomes:UP000320596}; RA Mcgann P., Snesrud E., Galac M.R.; RT "A Diverse Panel of Clinical Acinetobacter baumannii for Research Use."; RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases. RN [30] {ECO:0000313|EMBL:TWO50388.1, ECO:0000313|Proteomes:UP000320356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A42 {ECO:0000313|EMBL:TWO50388.1, RC ECO:0000313|Proteomes:UP000320356}; RA Ruan Z., Jia H.; RT "Draft genome sequence of Acinetobacter baumannii A42."; RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. The CC N-terminal methionine is often cleaved when the second residue in the CC primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, CC Thr, or Val). Requires deformylation of the N(alpha)-formylated CC initiator methionine before it can be hydrolyzed. {ECO:0000256|HAMAP- CC Rule:MF_01974}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of N-terminal amino acids, preferentially methionine, CC from peptides and arylamides.; EC=3.4.11.18; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974, CC ECO:0000256|RuleBase:RU003653}; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974, CC ECO:0000256|RuleBase:RU003653}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974, CC ECO:0000256|RuleBase:RU003653}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974, CC ECO:0000256|RuleBase:RU003653}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974, CC ECO:0000256|RuleBase:RU003653}; CC Note=Binds 2 divalent metal cations per subunit. Has a high-affinity CC and a low affinity metal-binding site. The true nature of the CC physiological cofactor is under debate. The enzyme is active with CC cobalt, zinc, manganese or divalent iron ions. Most likely, methionine CC aminopeptidases function as mononuclear Fe(2+)-metalloproteases under CC physiological conditions, and the catalytically relevant metal-binding CC site has been assigned to the histidine-containing high-affinity site. CC {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01974}. CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine CC aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01974}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP008706; AKA30982.1; -; Genomic_DNA. DR EMBL; CP021782; ASF78035.1; -; Genomic_DNA. DR EMBL; CP026125; AUT38008.1; -; Genomic_DNA. DR EMBL; CP027178; AVI33300.1; -; Genomic_DNA. DR EMBL; LRDW01000036; KZA22651.1; -; Genomic_DNA. DR EMBL; MDWM01000086; ODP71121.1; -; Genomic_DNA. DR EMBL; LYKI01000023; OIG72371.1; -; Genomic_DNA. DR EMBL; LYKQ01000028; OIH08354.1; -; Genomic_DNA. DR EMBL; NGCH01000216; OTL50035.1; -; Genomic_DNA. DR EMBL; NGEL01000129; OTM85450.1; -; Genomic_DNA. DR EMBL; NCYH01000005; OVL12321.1; -; Genomic_DNA. DR EMBL; NOXP01000002; OZT31344.1; -; Genomic_DNA. DR EMBL; NXDV01000014; PHQ01666.1; -; Genomic_DNA. DR EMBL; QKWF01000036; PZM18289.1; -; Genomic_DNA. DR EMBL; RFBY01000023; RSP76616.1; -; Genomic_DNA. DR EMBL; RFCO01000002; RSQ49839.1; -; Genomic_DNA. DR EMBL; RFDJ01000009; RSR10093.1; -; Genomic_DNA. DR EMBL; RXYO01000031; RTY10994.1; -; Genomic_DNA. DR EMBL; SEUD01000002; RYL18680.1; -; Genomic_DNA. DR EMBL; SEUE01000002; RYL31564.1; -; Genomic_DNA. DR EMBL; SEUG01000001; RYL46242.1; -; Genomic_DNA. DR EMBL; UFLV01000015; SSS24419.1; -; Genomic_DNA. DR EMBL; UFMQ01000008; SST23566.1; -; Genomic_DNA. DR EMBL; UFNX01000008; SSU74255.1; -; Genomic_DNA. DR EMBL; UFSC01000003; SUU32078.1; -; Genomic_DNA. DR EMBL; SNVS01000103; TEX13795.1; -; Genomic_DNA. DR EMBL; SNVP01000116; TEX30240.1; -; Genomic_DNA. DR EMBL; SSBA01000072; TGY98765.1; -; Genomic_DNA. DR EMBL; SRZJ01000037; TGZ07088.1; -; Genomic_DNA. DR EMBL; RFBA02000001; THJ60216.1; -; Genomic_DNA. DR EMBL; VAGE01000010; TLT63582.1; -; Genomic_DNA. DR EMBL; VAFZ01000011; TLT67225.1; -; Genomic_DNA. DR EMBL; VHEA01000004; TPS05618.1; -; Genomic_DNA. DR EMBL; VHEY01000019; TPS87062.1; -; Genomic_DNA. DR EMBL; VHFD01000006; TPS97919.1; -; Genomic_DNA. DR EMBL; VHGJ01000009; TPU23229.1; -; Genomic_DNA. DR EMBL; VHGY01000042; TPU61657.1; -; Genomic_DNA. DR EMBL; VHGX01000005; TPU81270.1; -; Genomic_DNA. DR EMBL; VNWR01000013; TWO50388.1; -; Genomic_DNA. DR RefSeq; WP_001089491.1; NZ_WIVO01000004.1. DR PDB; 6MRF; X-ray; 1.65 A; A=12-272. DR PDBsum; 6MRF; -. DR STRING; 470.IX87_07995; -. DR EnsemblBacteria; AIL78573; AIL78573; IX87_07995. DR EnsemblBacteria; AKA30982; AKA30982; ABUW_1234. DR EnsemblBacteria; AKQ26271; AKQ26271; ACX60_05910. DR EnsemblBacteria; AMN02327; AMN02327; AZE33_14285. DR EnsemblBacteria; BAP65968; BAP65968; IOMTU433_1184. DR EnsemblBacteria; KMV05062; KMV05062; AB895_0353. DR EnsemblBacteria; KMV10717; KMV10717; AB988_0028. DR EnsemblBacteria; KQD20501; KQD20501; APD06_11055. DR EnsemblBacteria; KQK46469; KQK46469; AQ482_07905. DR EnsemblBacteria; KUI76164; KUI76164; AQ480_02225. DR EnsemblBacteria; KZA22651; KZA22651; LV38_03303. DR EnsemblBacteria; OBE59901; OBE59901; A7934_09120. DR EnsemblBacteria; ODP71121; ODP71121; BGC29_02575. DR GeneID; 31348596; -. DR KEGG; abaa:IX88_14615; -. DR KEGG; abau:IX87_07995; -. DR KEGG; abk:LX00_12565; -. DR KEGG; abw:BL01_08915; -. DR PATRIC; fig|470.1288.peg.1761; -. DR eggNOG; ENOG4105CA1; Bacteria. DR eggNOG; COG0024; LUCA. DR KO; K01265; -. DR OrthoDB; 1285136at2; -. DR Proteomes; UP000032746; Chromosome. DR Proteomes; UP000076314; Unassembled WGS sequence. DR Proteomes; UP000094982; Unassembled WGS sequence. DR Proteomes; UP000179791; Unassembled WGS sequence. DR Proteomes; UP000179937; Unassembled WGS sequence. DR Proteomes; UP000194699; Unassembled WGS sequence. DR Proteomes; UP000194957; Unassembled WGS sequence. DR Proteomes; UP000195460; Unassembled WGS sequence. DR Proteomes; UP000197701; Chromosome. DR Proteomes; UP000216874; Unassembled WGS sequence. DR Proteomes; UP000223291; Unassembled WGS sequence. DR Proteomes; UP000236385; Chromosome. DR Proteomes; UP000248662; Unassembled WGS sequence. DR Proteomes; UP000252694; Unassembled WGS sequence. DR Proteomes; UP000253591; Unassembled WGS sequence. DR Proteomes; UP000255154; Unassembled WGS sequence. DR Proteomes; UP000257523; Chromosome. DR Proteomes; UP000264160; Unassembled WGS sequence. DR Proteomes; UP000269597; Unassembled WGS sequence. DR Proteomes; UP000271711; Unassembled WGS sequence. DR Proteomes; UP000272401; Unassembled WGS sequence. DR Proteomes; UP000278858; Unassembled WGS sequence. DR Proteomes; UP000280982; Unassembled WGS sequence. DR Proteomes; UP000291489; Unassembled WGS sequence. DR Proteomes; UP000292081; Unassembled WGS sequence. DR Proteomes; UP000292122; Unassembled WGS sequence. DR Proteomes; UP000297480; Unassembled WGS sequence. DR Proteomes; UP000297782; Unassembled WGS sequence. DR Proteomes; UP000306363; Unassembled WGS sequence. DR Proteomes; UP000307835; Unassembled WGS sequence. DR Proteomes; UP000309525; Unassembled WGS sequence. DR Proteomes; UP000310129; Unassembled WGS sequence. DR Proteomes; UP000315888; Unassembled WGS sequence. DR Proteomes; UP000318271; Unassembled WGS sequence. DR Proteomes; UP000318526; Unassembled WGS sequence. DR Proteomes; UP000318586; Unassembled WGS sequence. DR Proteomes; UP000320149; Unassembled WGS sequence. DR Proteomes; UP000320356; Unassembled WGS sequence. DR Proteomes; UP000320596; Unassembled WGS sequence. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule. DR CDD; cd01086; MetAP1; 1. DR Gene3D; 3.90.230.10; -; 1. DR HAMAP; MF_01974; MetAP_1; 1. DR InterPro; IPR036005; Creatinase/aminopeptidase-like. DR InterPro; IPR000994; Pept_M24. DR InterPro; IPR001714; Pept_M24_MAP. DR InterPro; IPR002467; Pept_M24A_MAP1. DR Pfam; PF00557; Peptidase_M24; 1. DR PRINTS; PR00599; MAPEPTIDASE. DR SUPFAM; SSF55920; SSF55920; 1. DR TIGRFAMs; TIGR00500; met_pdase_I; 1. DR PROSITE; PS00680; MAP_1; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:6MRF}; KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000256|RuleBase:RU003653, ECO:0000313|EMBL:PZM18289.1}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000313|EMBL:PZM18289.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000256|RuleBase:RU003653}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653}. FT DOMAIN 19..256 FT /note="Peptidase_M24" FT /evidence="ECO:0000259|Pfam:PF00557" FT METAL 110 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT METAL 121 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT METAL 121 FT /note="Divalent metal cation 2; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT METAL 185 FT /note="Divalent metal cation 2; catalytic; via tele FT nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT METAL 218 FT /note="Divalent metal cation 2; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT METAL 249 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT METAL 249 FT /note="Divalent metal cation 2; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT BINDING 92 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT BINDING 192 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" SQ SEQUENCE 275 AA; 30374 MW; 6D82AB2AE6DC1802 CRC64; MNSTYTAPRR LIKTPDEIEK MRIAGRLAAE VLDMIKPHIK AGVSTLELDT ICRNHIENVQ HAIPACVGYG GAPGRPAFQH SICTSVNHVV CHGIPSENKI LKNGDILNID VTVIKDGYHG DTNMMYIVGG ETSILANRLC KVAQEAMYRG MATVRDGSYL GDIGHAIQKY VESERFSVVR EYCGHGIGTV FHDEPQVLHY GQAGTGMRLE AGMTFTIEPM VNAGVWQTKL LGDKWTVVTK DHKLSAQYEH TILVTKTGIE VLTARPEEDL SRFNQ //