ID V5VCW7_ACIBA Unreviewed; 275 AA. AC V5VCW7; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 23-MAY-2018, entry version 48. 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:AUT38008.1}; 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=A7A65_11205 {ECO:0000313|EMBL:OWW98854.1}, A7M79_08180 GN {ECO:0000313|EMBL:OIH08354.1}, A7M90_04815 GN {ECO:0000313|EMBL:OIG72371.1}, A7N09_12540 GN {ECO:0000313|EMBL:OIF74617.1}, AB895_0353 GN {ECO:0000313|EMBL:KMV05062.1}, ABUW_1234 GN {ECO:0000313|EMBL:AKA30982.1}, APD06_11055 GN {ECO:0000313|EMBL:KQD20501.1}, AZE33_14285 GN {ECO:0000313|EMBL:AMN02327.1}, 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}, BWP00_06705 GN {ECO:0000313|EMBL:OOD23107.1}, C2U32_08280 GN {ECO:0000313|EMBL:AUT38008.1}, CBE85_00465 GN {ECO:0000313|EMBL:OWK68248.1}, CBI29_02666 GN {ECO:0000313|EMBL:ASF78035.1}, CEJ63_06330 GN {ECO:0000313|EMBL:PAM74467.1}, CHQ89_03925 GN {ECO:0000313|EMBL:OZT31344.1}, CPI82_15740 GN {ECO:0000313|EMBL:PHQ01666.1}, IX87_07995 GN {ECO:0000313|EMBL:AIL78573.1}, LV38_03303 GN {ECO:0000313|EMBL:KZA22651.1}; OS Acinetobacter baumannii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=470 {ECO:0000313|EMBL:KQD20501.1, ECO:0000313|Proteomes:UP000051322}; RN [1] {ECO:0000313|EMBL:AIL78573.1, ECO:0000313|Proteomes:UP000028932} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB030 {ECO:0000313|EMBL:AIL78573.1}, and AB30 RC {ECO:0000313|Proteomes:UP000028932}; RA Loewen P.C., Kumar A.; RT "Genome sequence of Acinetobacter baumannii AB030 genome."; RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AKA30982.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB5075-UW {ECO:0000313|EMBL:AKA30982.1}; RX PubMed=25845845; RA Gallagher L.A., Ramage E., Weiss E.J., Radey M., Hayden H.S., RA Held K.G., 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., RA Radey M.R., 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:CQR89265.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CHI-32 {ECO:0000313|EMBL:CQR89265.1}; RA Jones S Lim; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:KMV05062.1, ECO:0000313|Proteomes:UP000036720} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B8342 {ECO:0000313|EMBL:KMV05062.1, RC ECO:0000313|Proteomes:UP000036720}; RA Vijaykumar S., Balaji V., Biswas I.; RT "Complete genome sequence of Acinetobacter baumannii strain B8342, a RT motility positive clinical isolate."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:KQD20501.1, ECO:0000313|Proteomes:UP000051322} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABBL059 {ECO:0000313|EMBL:KQD20501.1, RC ECO:0000313|Proteomes:UP000051322}; RA Ozer E.A., Fitzpatrick M.A., Hauser A.R.; RT "The utility of whole genome sequencing in characterizing RT Acinetobacter epidemiology and analyzing hospital outbreaks."; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [7] {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 RT military personnel."; RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:AMN02327.1, ECO:0000313|Proteomes:UP000070590} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XH858 {ECO:0000313|EMBL:AMN02327.1, RC ECO:0000313|Proteomes:UP000070590}; RA Feng Y., Hua X., Yu Y.; RT "Complete genome of Acinetobacter baumannii str. XH858."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|Proteomes:UP000179770, 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}, XH647 RC {ECO:0000313|EMBL:OIG72371.1, ECO:0000313|Proteomes:UP000179937}, and RC XH694 {ECO:0000313|EMBL:OIF74617.1, RC ECO:0000313|Proteomes:UP000179770}; RA Hua X., Yu Y.; RT "The evolution of Acinetobacter baumannii in vivo."; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:OWW98854.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AB314 {ECO:0000313|EMBL:OWW98854.1}; RA Lavstsen T., Jespersen J.S.; RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases. RN [11] {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 RT of Acinetobacter baumannii."; RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases. RN [12] {ECO:0000313|EMBL:OOD23107.1, ECO:0000313|Proteomes:UP000188718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17945 {ECO:0000313|EMBL:OOD23107.1, RC ECO:0000313|Proteomes:UP000188718}; RA Kozyreva V.K., Truong C.-L., Greninger A.L., Mukhopadhyay R., RA Crandall J., Chaturvedi V.; RT "Validation and Implementation of CLIA-Compliant Whole Genome RT Sequencing (WGS) in Public Health Laboratory."; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. RN [13] {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 [14] {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 [15] {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 [16] {ECO:0000313|EMBL:PAM74467.1, ECO:0000313|Proteomes:UP000216072} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB75 {ECO:0000313|EMBL:PAM74467.1, RC ECO:0000313|Proteomes:UP000216072}; RA Chen Q.; RT "Carbapenem-resistant Acinetobacter baumannii strains."; RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases. RN [17] {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 RT belonging to global clone 1 (GC1)."; RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases. RN [18] {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 [19] {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 RT resistant bacteria."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. RN [20] {ECO:0000313|EMBL:AUT38008.1, ECO:0000313|Proteomes:UP000236385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABNIH28 {ECO:0000313|EMBL:AUT38008.1, RC ECO:0000313|Proteomes:UP000236385}; 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 [21] {ECO:0000313|EMBL:AUT38008.1, ECO:0000313|Proteomes:UP000236385} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ABNIH28 {ECO:0000313|EMBL:AUT38008.1, RC ECO:0000313|Proteomes:UP000236385}; RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.; RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids, CC preferentially methionine, from peptides and arylamides. CC {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653}. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01974, ECO:0000256|RuleBase:RU003653}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01974, ECO:0000256|RuleBase:RU003653}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01974, ECO:0000256|RuleBase:RU003653}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01974, ECO:0000256|RuleBase:RU003653}; CC Note=Binds 2 divalent metal cations per subunit. Has a high- CC affinity and a low affinity metal-binding site. The true nature of CC the physiological cofactor is under debate. The enzyme is active CC with cobalt, zinc, manganese or divalent iron ions. Most likely, CC methionine aminopeptidases function as mononuclear Fe(2+)- CC metalloproteases under physiological conditions, and the CC catalytically relevant metal-binding site has been assigned to the CC histidine-containing high-affinity site. {ECO:0000256|HAMAP- CC Rule:MF_01974, ECO:0000256|RuleBase:RU003653}; CC -!- SUBUNIT: Monomer. {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; CP009257; AIL78573.1; -; Genomic_DNA. DR EMBL; CP008706; AKA30982.1; -; Genomic_DNA. DR EMBL; CP014528; AMN02327.1; -; Genomic_DNA. DR EMBL; CP021782; ASF78035.1; -; Genomic_DNA. DR EMBL; CP026125; AUT38008.1; -; Genomic_DNA. DR EMBL; CVLF01000087; CQR89265.1; -; Genomic_DNA. DR EMBL; LFYZ01000001; KMV05062.1; -; Genomic_DNA. DR EMBL; LLFE01000041; KQD20501.1; -; Genomic_DNA. DR EMBL; LRDW01000036; KZA22651.1; -; Genomic_DNA. DR EMBL; MDWM01000086; ODP71121.1; -; Genomic_DNA. DR EMBL; LYIX01002080; OIF74617.1; -; Genomic_DNA. DR EMBL; LYKI01000023; OIG72371.1; -; Genomic_DNA. DR EMBL; LYKQ01000028; OIH08354.1; -; Genomic_DNA. DR EMBL; MTGG01000011; OOD23107.1; -; 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; NGKM01000001; OWK68248.1; -; Genomic_DNA. DR EMBL; LYNJ01000237; OWW98854.1; -; Genomic_DNA. DR EMBL; NOXP01000002; OZT31344.1; -; Genomic_DNA. DR EMBL; NKKG01000021; PAM74467.1; -; Genomic_DNA. DR EMBL; NXDV01000014; PHQ01666.1; -; Genomic_DNA. DR RefSeq; WP_001089491.1; NZ_PUDP01000004.1. 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 Proteomes; UP000028932; Chromosome. DR Proteomes; UP000032746; Chromosome. DR Proteomes; UP000036720; Unassembled WGS sequence. DR Proteomes; UP000051322; Unassembled WGS sequence. DR Proteomes; UP000070590; Chromosome. DR Proteomes; UP000076314; Unassembled WGS sequence. DR Proteomes; UP000094982; Unassembled WGS sequence. DR Proteomes; UP000179770; Unassembled WGS sequence. DR Proteomes; UP000179791; Unassembled WGS sequence. DR Proteomes; UP000179937; Unassembled WGS sequence. DR Proteomes; UP000188718; Unassembled WGS sequence. DR Proteomes; UP000194699; Unassembled WGS sequence. DR Proteomes; UP000194957; Unassembled WGS sequence. DR Proteomes; UP000195460; Unassembled WGS sequence. DR Proteomes; UP000197394; Unassembled WGS sequence. DR Proteomes; UP000197701; Chromosome. DR Proteomes; UP000216072; Unassembled WGS sequence. DR Proteomes; UP000216874; Unassembled WGS sequence. DR Proteomes; UP000223291; Unassembled WGS sequence. DR Proteomes; UP000236385; Chromosome. 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 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 3: Inferred from homology; KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000256|RuleBase:RU003653, ECO:0000313|EMBL:KQD20501.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000028932, KW ECO:0000313|Proteomes:UP000032746, ECO:0000313|Proteomes:UP000036720, KW ECO:0000313|Proteomes:UP000051322}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000313|EMBL:KQD20501.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000256|RuleBase:RU003653}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000256|RuleBase:RU003653}. FT DOMAIN 19 256 Peptidase_M24. {ECO:0000259|Pfam: FT PF00557}. FT METAL 110 110 Divalent metal cation 1. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 121 121 Divalent metal cation 1. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 121 121 Divalent metal cation 2; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 185 185 Divalent metal cation 2; catalytic; via FT tele nitrogen. {ECO:0000256|HAMAP-Rule: FT MF_01974}. FT METAL 218 218 Divalent metal cation 2; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 249 249 Divalent metal cation 1. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT METAL 249 249 Divalent metal cation 2; catalytic. FT {ECO:0000256|HAMAP-Rule:MF_01974}. FT BINDING 92 92 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01974}. FT BINDING 192 192 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //