ID V5VCW7_ACIBA Unreviewed; 275 AA. AC V5VCW7; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 24-JUL-2024, entry version 89. 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}, map3 GN {ECO:0000313|EMBL:CUW35909.1}, map_2 {ECO:0000313|EMBL:KZA12740.1}; GN ORFNames=A7M90_04815 {ECO:0000313|EMBL:OIG72371.1}, ABR2091_2512 GN {ECO:0000313|EMBL:CUW35909.1}, ABUW_1234 GN {ECO:0000313|EMBL:AKA30982.1}, APD17_10230 GN {ECO:0000313|EMBL:KQD54506.1}, AUO97_00550 GN {ECO:0000313|EMBL:APP29388.1}, B9W25_05720 GN {ECO:0000313|EMBL:PRN35987.1}, B9X95_11705 GN {ECO:0000313|EMBL:OTM85450.1}, CBE85_00465 GN {ECO:0000313|EMBL:OWK68248.1}, CV954_005965 GN {ECO:0000313|EMBL:PQL84274.1}, DOL94_04640 GN {ECO:0000313|EMBL:PZM18289.1}, EA706_00955 GN {ECO:0000313|EMBL:RSQ49839.1}, EA722_08630 GN {ECO:0000313|EMBL:RSP76616.1}, EJ507_19900 GN {ECO:0000313|EMBL:RTB85817.1}, F2P40_02010 GN {ECO:0000313|EMBL:MQR48113.1}, F4T85_00585 GN {ECO:0000313|EMBL:MQZ66891.1}, FJU42_15260 GN {ECO:0000313|EMBL:TPU61657.1}, G3N53_09925 GN {ECO:0000313|EMBL:NDW41392.1}, GNY86_13630 GN {ECO:0000313|EMBL:MVM92566.1}, GSE42_14095 GN {ECO:0000313|EMBL:MYM79056.1}, IAG11_02480 GN {ECO:0000313|EMBL:MBD0218758.1}, IMO23_12425 GN {ECO:0000313|EMBL:QPF12406.1}, ITE13_14325 GN {ECO:0000313|EMBL:MBP4960678.1}, LV35_03405 GN {ECO:0000313|EMBL:KZA12740.1}, MKP18_000955 GN {ECO:0000313|EMBL:EKU3567577.1}, P9867_17035 GN {ECO:0000313|EMBL:MDK4883330.1}, SAMEA104305318_02021 GN {ECO:0000313|EMBL:SST23566.1}, SAMEA4394745_01927 GN {ECO:0000313|EMBL:SSI43005.1}; OS Acinetobacter baumannii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae; OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=470 {ECO:0000313|EMBL:PZM18289.1, ECO:0000313|Proteomes:UP000248662}; RN [1] {ECO:0000313|EMBL:APP29388.1, ECO:0000313|Proteomes:UP000072389} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17978 {ECO:0000313|Proteomes:UP000072389}, and ATCC RC 17978-VU {ECO:0000313|EMBL:APP29388.1}; RX PubMed=25136007; DOI=10.1128/AAC.03074-14; RA Fernando D.M., Xu W., Loewen P.C., Zhanel G.G., Kumar A.; RT "Triclosan can select for an AdeIJK-overexpressing mutant of Acinetobacter RT baumannii ATCC 17978 that displays reduced susceptibility to multiple RT antibiotics."; RL Antimicrob. Agents Chemother. 58:6424-6431(2014). RN [2] {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 [3] {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 [4] {ECO:0000313|EMBL:KQD54506.1, ECO:0000313|Proteomes:UP000051023} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABBL067b {ECO:0000313|EMBL:KQD54506.1, RC ECO:0000313|Proteomes:UP000051023}; RA Ozer E.A., Fitzpatrick M.A., Hauser A.R.; RT "The utility of whole genome sequencing in characterizing Acinetobacter RT epidemiology and analyzing hospital outbreaks."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:CUW35909.1, ECO:0000313|Proteomes:UP000066661} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R2091 {ECO:0000313|EMBL:CUW35909.1}; RA Wibberg D.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:APP29388.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17978-VU {ECO:0000313|EMBL:APP29388.1}; RA Singh M.K., Fernando D.M., Kumar A.; RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:KZA12740.1, ECO:0000313|Proteomes:UP000076296} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB2828 {ECO:0000313|EMBL:KZA12740.1, RC ECO:0000313|Proteomes:UP000076296}; 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 [8] {ECO:0000313|EMBL:OIG72371.1, ECO:0000313|Proteomes:UP000179937} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XH647 {ECO:0000313|EMBL:OIG72371.1, RC 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 [9] {ECO:0000313|EMBL:APP29388.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 17978-VU {ECO:0000313|EMBL:APP29388.1}; RA Singh M., Fernando D., Kumar A.; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:MYM79056.1, ECO:0000313|Proteomes:UP000480763} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DMS06669 {ECO:0000313|EMBL:MYM79056.1, RC ECO:0000313|Proteomes:UP000480763}; RX PubMed=29137647; RA Si-Tuan N., Ngoc H.M., Hang P.T.T., Nguyen C., Van P.H., Huong N.T.; RT "New eight genes identified at the clinical multidrug-resistant RT Acinetobacter baumannii DMS06669 strain in a Vietnam hospital."; RL Ann. Clin. Microbiol. Antimicrob. 16:0-74(2017). RN [11] {ECO:0000313|EMBL:PRN35987.1, ECO:0000313|Proteomes:UP000237823} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KUFAR57 {ECO:0000313|EMBL:PRN35987.1, RC ECO:0000313|Proteomes:UP000237823}; RA Nasser K., Habibi N., Khan M.W., Purohit P., Al-Obaid I., Dhar R., RA Al-Fouzan W., Mustafa A.S.; RT "Comparison of Acinetobacter baumannii whole genome sequences from two RT major hospitals in Kuwait."; RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases. RN [12] {ECO:0000313|EMBL:OWK68248.1, ECO:0000313|Proteomes:UP000197394} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB360 {ECO:0000313|EMBL:OWK68248.1, RC ECO:0000313|Proteomes:UP000197394}; RA Wareham D.W., Bean D.C.; RT "Draft genome sequence of MDR A. baumannii AB360."; RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases. RN [13] {ECO:0000313|EMBL:OTM85450.1, ECO:0000313|Proteomes:UP000194699} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PR350 {ECO:0000313|EMBL:OTM85450.1, RC ECO:0000313|Proteomes:UP000194699}; RA Song R., Chenine A.L., Ruprecht R.M.; RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases. RN [14] {ECO:0000313|EMBL:PQL84274.1, ECO:0000313|Proteomes:UP000233757} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ZQ8 {ECO:0000313|EMBL:PQL84274.1, RC ECO:0000313|Proteomes:UP000233757}; RA Qasim Z.J.; RT "Acinetobacter baumanii whole genome sequence."; RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases. RN [15] {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 [16] {ECO:0000313|Proteomes:UP000252694, ECO:0000313|Proteomes:UP000262697} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4300STDY6542375 {ECO:0000313|EMBL:SSI43005.1, RC ECO:0000313|Proteomes:UP000262697}, and 4300STDY7045823 RC {ECO:0000313|EMBL:SST23566.1, ECO:0000313|Proteomes:UP000252694}; RG Pathogen Informatics; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [17] {ECO:0007829|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 [18] {ECO:0000313|Proteomes:UP000269597, ECO:0000313|Proteomes:UP000272401} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TG22168 {ECO:0000313|EMBL:RSQ49839.1, RC ECO:0000313|Proteomes:UP000272401}, and TG31299 RC {ECO:0000313|EMBL:RSP76616.1, ECO:0000313|Proteomes:UP000269597}; 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 [19] {ECO:0000313|EMBL:RTB85817.1, ECO:0000313|Proteomes:UP000277944} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R348 {ECO:0000313|EMBL:RTB85817.1, RC ECO:0000313|Proteomes:UP000277944}; RA D'Souza R., Fouts D., Singh I., Nguyen K.; RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases. RN [20] {ECO:0000313|EMBL:TPU61657.1, ECO:0000313|Proteomes:UP000315888} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MRSN14237 {ECO:0000313|EMBL:TPU61657.1, RC ECO:0000313|Proteomes:UP000315888}; 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 [21] {ECO:0000313|EMBL:MQZ66891.1, ECO:0000313|Proteomes:UP000420346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AMA26 {ECO:0000313|EMBL:MQZ66891.1, RC ECO:0000313|Proteomes:UP000420346}; RA Maria R.S., Adams M.D.; RT "Distinct mechanisms of dissemination of NDM-1 metallo-beta-betalactamase RT in Acinetobacter species spp. in Argentina."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. RN [22] {ECO:0000313|EMBL:MQR48113.1, ECO:0000313|Proteomes:UP000461234} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABS103 {ECO:0000313|EMBL:MQR48113.1, RC ECO:0000313|Proteomes:UP000461234}; RA Douraghi M., Aris P., Kenyon J., Hamidian M.; RT "Genetic environment of the oxa23 gene and comparative analysis of RT carbapenem resistant Acinetobacter baumannii isolates belonging to global RT clone 1, lineage 2 recovered in a burns hospital outbreak in 2012-2013."; RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases. RN [23] {ECO:0000313|EMBL:MVM92566.1, ECO:0000313|Proteomes:UP000439424} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ac576 {ECO:0000313|EMBL:MVM92566.1, RC ECO:0000313|Proteomes:UP000439424}; RA Fedrigo N.H., Cerdeira L., Fuga B., Marini P.V.B., Shinohara D.R., RA Carrara-Marroni F.E., Lincopan N., Tognim M.C.B.; RT "Multidrug-resistant Acinetobacter baumannii moving toward extensively RT drug-resistant over fifteen years in South of Brazil."; RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases. RN [24] {ECO:0000313|EMBL:MYM79056.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DMS06669 {ECO:0000313|EMBL:MYM79056.1}; RA Nguyen S.-T.; RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases. RN [25] {ECO:0000313|EMBL:NDW41392.1, ECO:0000313|Proteomes:UP000470018} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SP816 {ECO:0000313|EMBL:NDW41392.1, RC ECO:0000313|Proteomes:UP000470018}; RA Veeraraghavan B., Mathur P., Vijayakumar S., Vasudevan K., Lincy M., RA Kirubananthan A.; RT "Whole genome shot-gun sequencing of clinical Carbapenem resistant A. RT baumannii."; RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases. RN [26] {ECO:0000313|EMBL:MBD0218758.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A86 {ECO:0000313|EMBL:MBD0218758.1}; RA Abouelfetouh A., Mattock J., Turner D., Li E., Evans B.A.; RT "Diversity of carbapenem-resistant Acinetobacter baumannii and RT bacteriophage-mediated spread of the Oxa23 carbapenemase."; RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases. RN [27] {ECO:0000313|EMBL:QPF12406.1, ECO:0000313|Proteomes:UP000594659} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Res13-Abat-PEA21-P4-01-A {ECO:0000313|EMBL:QPF12406.1, RC ECO:0000313|Proteomes:UP000594659}; RA Poulin-Laprade D., Brouard J.-S., Gagnon N., Turcotte A., Langlois A., RA Matte J.J., Carrillo C.D., Zaheer R., McAllister T., Topp E., Talbot G.; RT "Resistance determinants and their genetic context in bacteria from a RT longitudinal study of pigs reared under conventional and antibiotic-free RT husbandry practices."; RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases. RN [28] {ECO:0000313|EMBL:MBP4960678.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=E314 {ECO:0000313|EMBL:MBP4960678.1}; RA Frenk S., Rakovitsky N.; RT "Epidemiology and genetic characterization of 247 CRAB isolated from RT infections."; RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases. RN [29] {ECO:0000313|EMBL:MDK4883330.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CPO519 {ECO:0000313|EMBL:MDK4883330.1}; RA Macesic N.; RT "Genomic dissection of endemic carbapenem resistance: metallo-beta- RT lactamase gene dissemination through clonal, plasmid and integron transfer RT pathways."; RL Submitted (JAN-2023) to the EMBL/GenBank/DDBJ databases. RN [30] {ECO:0000313|EMBL:EMN1070674.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2021GN-00227 {ECO:0000313|EMBL:EKU3567577.1}; RG Clinical and Environmental Microbiology Branch: Whole genome sequencing antimicrobial resistance pathogens in the healthcare setting; RL Submitted (FEB-2024) 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. CC {ECO:0000256|ARBA:ARBA00002521, ECO:0000256|HAMAP-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 Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974}; 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}; 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; CP018664; APP29388.1; -; Genomic_DNA. DR EMBL; LN997846; CUW35909.1; -; Genomic_DNA. DR EMBL; ABFEVW020000005; EKU3567577.1; -; Genomic_DNA. DR EMBL; ABFEVW030000005; EMN1070674.1; -; Genomic_DNA. DR EMBL; LLFO01000047; KQD54506.1; -; Genomic_DNA. DR EMBL; LRDT01000044; KZA12740.1; -; Genomic_DNA. DR EMBL; JACSVK010000003; MBD0218758.1; -; Genomic_DNA. DR EMBL; JAEHMK010000019; MBP4960678.1; -; Genomic_DNA. DR EMBL; JARTMM010000087; MDK4883330.1; -; Genomic_DNA. DR EMBL; WIOC01000002; MQR48113.1; -; Genomic_DNA. DR EMBL; VYTH01000001; MQZ66891.1; -; Genomic_DNA. DR EMBL; WPIP01000105; MVM92566.1; -; Genomic_DNA. DR EMBL; WWCH01000001; MYM79056.1; -; Genomic_DNA. DR EMBL; JAAGTY010000009; NDW41392.1; -; Genomic_DNA. DR EMBL; LYKI01000023; OIG72371.1; -; Genomic_DNA. DR EMBL; NGEL01000129; OTM85450.1; -; Genomic_DNA. DR EMBL; NGKM01000001; OWK68248.1; -; Genomic_DNA. DR EMBL; PHJU02000014; PQL84274.1; -; Genomic_DNA. DR EMBL; NEPB01000008; PRN35987.1; -; Genomic_DNA. DR EMBL; QKWF01000036; PZM18289.1; -; Genomic_DNA. DR EMBL; CP062919; QPF12406.1; -; Genomic_DNA. DR EMBL; RFBY01000023; RSP76616.1; -; Genomic_DNA. DR EMBL; RFCO01000002; RSQ49839.1; -; Genomic_DNA. DR EMBL; RWXH01000089; RTB85817.1; -; Genomic_DNA. DR EMBL; UFDJ01000008; SSI43005.1; -; Genomic_DNA. DR EMBL; UFMQ01000008; SST23566.1; -; Genomic_DNA. DR EMBL; VHGY01000042; TPU61657.1; -; Genomic_DNA. DR RefSeq; WP_001089491.1; NZ_WYAT01000001.1. DR PDB; 6MRF; X-ray; 1.65 A; A=12-272. DR PDBsum; 6MRF; -. DR STRING; 1096995.BJAB07104_02683; -. DR GeneID; 66396496; -. DR KEGG; abw:BL01_08915; -. DR PATRIC; fig|470.1288.peg.1761; -. DR eggNOG; COG0024; Bacteria. DR OMA; FYGDHAY; -. DR OrthoDB; 9802055at2; -. DR Proteomes; UP000032746; Chromosome. DR Proteomes; UP000051023; Unassembled WGS sequence. DR Proteomes; UP000066661; Chromosome I. DR Proteomes; UP000072389; Chromosome. DR Proteomes; UP000076296; Unassembled WGS sequence. DR Proteomes; UP000179937; Unassembled WGS sequence. DR Proteomes; UP000194699; Unassembled WGS sequence. DR Proteomes; UP000197394; Unassembled WGS sequence. DR Proteomes; UP000233757; Unassembled WGS sequence. DR Proteomes; UP000237823; Unassembled WGS sequence. DR Proteomes; UP000248662; Unassembled WGS sequence. DR Proteomes; UP000252694; Unassembled WGS sequence. DR Proteomes; UP000262697; Unassembled WGS sequence. DR Proteomes; UP000269597; Unassembled WGS sequence. DR Proteomes; UP000272401; Unassembled WGS sequence. DR Proteomes; UP000277944; Unassembled WGS sequence. DR Proteomes; UP000315888; Unassembled WGS sequence. DR Proteomes; UP000420346; Unassembled WGS sequence. DR Proteomes; UP000439424; Unassembled WGS sequence. DR Proteomes; UP000461234; Unassembled WGS sequence. DR Proteomes; UP000470018; Unassembled WGS sequence. DR Proteomes; UP000480763; Unassembled WGS sequence. DR Proteomes; UP000594659; Chromosome. DR Proteomes; UP000634608; Unassembled WGS sequence. DR Proteomes; UP000673677; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004239; F:initiator methionyl aminopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046914; F:transition metal ion binding; IEA:UniProt. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd01086; MetAP1; 1. DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 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 NCBIfam; TIGR00500; met_pdase_I; 1. DR PANTHER; PTHR43330; METHIONINE AMINOPEPTIDASE; 1. DR PANTHER; PTHR43330:SF8; METHIONINE AMINOPEPTIDASE 1D, MITOCHONDRIAL; 1. DR Pfam; PF00557; Peptidase_M24; 1. DR PRINTS; PR00599; MAPEPTIDASE. DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1. DR PROSITE; PS00680; MAP_1; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:6MRF}; KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000256|RuleBase:RU003653}; 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 BINDING 92 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT BINDING 110 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT BINDING 121 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT BINDING 121 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT BINDING 185 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT BINDING 192 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT BINDING 218 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT BINDING 249 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT BINDING 249 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" 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 //