ID V5VCW7_ACIBA Unreviewed; 275 AA. AC V5VCW7; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 11-NOV-2015, entry version 20. DE RecName: Full=Methionine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974}; 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}; DE AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_01974}; GN Name=map1 {ECO:0000313|EMBL:AKA30982.1}; GN Synonyms=map {ECO:0000256|HAMAP-Rule:MF_01974, GN ECO:0000313|EMBL:BAP65968.1}, map3 {ECO:0000313|EMBL:CRL95227.1}; GN ORFNames=AB895_0353 {ECO:0000313|EMBL:KMV05062.1}, AB987_2690 GN {ECO:0000313|EMBL:KMV27219.1}, AB988_0028 GN {ECO:0000313|EMBL:KMV10717.1}, AB994_1981 GN {ECO:0000313|EMBL:KMV03238.1}, ABCIP7010_2514 GN {ECO:0000313|EMBL:CRL95227.1}, ABR2090_1208 GN {ECO:0000313|EMBL:CRX64132.1}, ABUW_1234 GN {ECO:0000313|EMBL:AKA30982.1}, ACX60_05910 GN {ECO:0000313|EMBL:AKQ26271.1}, AKG97_01110 GN {ECO:0000313|EMBL:KOP89520.1}, IOMTU433_1184 GN {ECO:0000313|EMBL:BAP65968.1}, IX87_07995 GN {ECO:0000313|EMBL:AIL78573.1}, LH92_12295 GN {ECO:0000313|EMBL:KGF60633.1}, RP89_09635 GN {ECO:0000313|EMBL:KIA15515.1}, RQ24_04615 GN {ECO:0000313|EMBL:KJG81168.1}, RQ37_03770 GN {ECO:0000313|EMBL:KJE63625.1}, RQ42_05190 GN {ECO:0000313|EMBL:KJE61738.1}, RQ49_01840 GN {ECO:0000313|EMBL:KJF15001.1}, RQ64_07755 GN {ECO:0000313|EMBL:KJF11281.1}, RQ80_13680 GN {ECO:0000313|EMBL:KJG77179.1}, RQ82_03725 GN {ECO:0000313|EMBL:KJG75542.1}, RQ85_11030 GN {ECO:0000313|EMBL:KHX40556.1}, RQ98_01200 GN {ECO:0000313|EMBL:KJE73081.1}, RR20_01165 GN {ECO:0000313|EMBL:KJE68647.1}, RR21_08695 GN {ECO:0000313|EMBL:KJF02887.1}, RR22_11905 GN {ECO:0000313|EMBL:KJF05880.1}, RR27_02775 GN {ECO:0000313|EMBL:KJE74574.1}, RU84_05625 GN {ECO:0000313|EMBL:AJB66358.1}, RW49_11850 GN {ECO:0000313|EMBL:KHT85672.1}, RW53_02290 GN {ECO:0000313|EMBL:KHT74985.1}, RW56_05425 GN {ECO:0000313|EMBL:KHV22247.1}, RW57_01585 GN {ECO:0000313|EMBL:KHV28669.1}, RW58_12575 GN {ECO:0000313|EMBL:KHV33855.1}, RW59_04665 GN {ECO:0000313|EMBL:KHV18126.1}, RW60_02595 GN {ECO:0000313|EMBL:KHV33176.1}, TE32_05490 GN {ECO:0000313|EMBL:AKJ45008.1}, UN98_08720 GN {ECO:0000313|EMBL:KKZ40688.1}, UO01_16465 GN {ECO:0000313|EMBL:KKZ44945.1}, VM83_11790 GN {ECO:0000313|EMBL:KKA96472.1}; OS Acinetobacter baumannii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Acinetobacter; OC Acinetobacter calcoaceticus/baumannii complex. OX NCBI_TaxID=470 {ECO:0000313|EMBL:KHX40556.1}; 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:KGF60633.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MAR002 {ECO:0000313|EMBL:KGF60633.1}; RA Alvarez-Fraga L., Rumbo-Feal S., Merino M., Bou G., Poza M.; RT "Complete genome of a biofilm superproducing strain of Acinetobacter RT baumannii."; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:BAP65968.1, ECO:0000313|Proteomes:UP000031644} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IOMTU 433 {ECO:0000313|EMBL:BAP65968.1, RC ECO:0000313|Proteomes:UP000031644}; RA Tada T., Shrestha S., Miyoshi-Akiyama T., Shimada K., Kirikae T.; RT "Complete genome sequence of Acinetobacter baumannii IOMTU433."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:AJB66358.1, ECO:0000313|Proteomes:UP000031136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=6200 {ECO:0000313|EMBL:AJB66358.1, RC ECO:0000313|Proteomes:UP000031136}; RA McCorrison J., Sanka R., Adams M., Brinkac L., Sutton G., Bonomo R., RA Rojas L.; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:AKJ45008.1, ECO:0000313|Proteomes:UP000035522} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=XH386 {ECO:0000313|EMBL:AKJ45008.1, RC ECO:0000313|Proteomes:UP000035522}; RA Fang Y., Hua X., Feng Y., Lil X., Weng J., Ruan Z., Shang S., Yu Y.; RT "Complete genome sequence of a multi-drug resistant ST208 RT Acinetobacter baumannii."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:KKZ40688.1, ECO:0000313|Proteomes:UP000033888, ECO:0000313|Proteomes:UP000034216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=161/07 {ECO:0000313|EMBL:KKZ44945.1, RC ECO:0000313|Proteomes:UP000034216}, and LUH_7841 RC {ECO:0000313|EMBL:KKZ40688.1, ECO:0000313|Proteomes:UP000033888}; RA Sahl J., Zarrilli R.; RT "Genomic epidemiology of Acinetobacter baumannii strains assigned to RT the ST25 clonal lineage; the evolution of a globally relevant clone."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:KKA96472.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=718532 {ECO:0000313|EMBL:KKA96472.1}; RA Yim A.K., Leung A.K., Yu A.C.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. RN [8] {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}; 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 [9] {ECO:0000313|EMBL:KKA96472.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=718532 {ECO:0000313|EMBL:KKA96472.1}; RA Tsui S.K., Ip M., Chan T.-F., Kwok J.S.; RT "Draft Genome of a Resistant Acinetobacter baumannii Strain from a RT Patient in Hong Kong, China."; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:CQR67878.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CHI-32 {ECO:0000313|EMBL:CQR89265.1}, CHI-34 RC {ECO:0000313|EMBL:CRF38470.1}, and CHI-45-1 RC {ECO:0000313|EMBL:CQR67878.1}; RA Jones S Lim; RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|EMBL:CRL95227.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CIP70.10 {ECO:0000313|EMBL:CRL95227.1}, and R2090 RC {ECO:0000313|EMBL:CRX64132.1}; RA Wibberg Daniel; RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases. RN [12] {ECO:0000313|EMBL:AKQ26271.1, ECO:0000313|Proteomes:UP000036024} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17978-mff {ECO:0000313|EMBL:AKQ26271.1, RC ECO:0000313|Proteomes:UP000036024}; RA Weber B.S., Ly P.M., Irwin J.N., Pukatzki S., Feldman M.F.; RT "A multidrug resistance plasmid contains the molecular switch for type RT VI secretion in Acinetobacter baumannii."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [13] {ECO:0000313|EMBL:KMV27219.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B8300 {ECO:0000313|EMBL:KMV27219.1}; RA Vijaykumar S., Balaji V., Biswas I.; RT "Complete genome sequence of Acinetobacter baumannii strain B8300 that RT displays high twitching motility."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [14] {ECO:0000313|EMBL:KMV05062.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B8342 {ECO:0000313|EMBL:KMV05062.1}; 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 [15] {ECO:0000313|EMBL:KMV03238.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B11911 {ECO:0000313|EMBL:KMV03238.1}, and SP1917 RC {ECO:0000313|EMBL:KMV10717.1}; RA Vijaykumar S., Balaji V., Biswas I.; RT "Draft genome sequences of two multidrug resistant Acinetobacter RT baumannii isolates from Southern India."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [16] {ECO:0000313|EMBL:KHX40556.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=10441_14 {ECO:0000313|EMBL:KOP89520.1}, ABUH304350 RC {ECO:0000313|EMBL:KHV18126.1}, ABUH304352 RC {ECO:0000313|EMBL:KHV28669.1}, ABUH404571 RC {ECO:0000313|EMBL:KHV33855.1}, ABUH42783 RC {ECO:0000313|EMBL:KHT85672.1}, ABUH463346 RC {ECO:0000313|EMBL:KHV22247.1}, ABUH4837 {ECO:0000313|EMBL:KHT74985.1}, RC ABUH524354 {ECO:0000313|EMBL:KHV33176.1}, UH175_674 RC {ECO:0000313|EMBL:KJE74574.1}, UH17_151 {ECO:0000313|EMBL:KJG81168.1}, RC UH225_433 {ECO:0000313|EMBL:KJG75542.1}, UH326_445 RC {ECO:0000313|EMBL:KHX40556.1}, UH381_484 RC {ECO:0000313|EMBL:KJE73081.1}, UH475_361 RC {ECO:0000313|EMBL:KJF11281.1}, UH514_289 RC {ECO:0000313|EMBL:KJF15001.1}, UH535_423 RC {ECO:0000313|EMBL:KJG77179.1}, UH592_583 RC {ECO:0000313|EMBL:KJE68647.1}, UH592_595 RC {ECO:0000313|EMBL:KJF02887.1}, UH592_599 RC {ECO:0000313|EMBL:KJF05880.1}, UH66_253 {ECO:0000313|EMBL:KJE63625.1}, RC and UH66_271 {ECO:0000313|EMBL:KJE61738.1}; RA Tran T., Druce J.; RT "MeaNS - Measles Nucleotide Surveillance Program."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [17] {ECO:0000313|EMBL:KIA15515.1, ECO:0000313|Proteomes:UP000031375} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UH17_52 {ECO:0000313|EMBL:KIA15515.1, RC ECO:0000313|Proteomes:UP000031375}; RA Noorani M.; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. RN [18] {ECO:0000313|Proteomes:UP000031375, ECO:0000313|Proteomes:UP000033888, ECO:0000313|Proteomes:UP000034216} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=161/07 {ECO:0000313|Proteomes:UP000034216}, LUH_7841 RC {ECO:0000313|Proteomes:UP000033888}, and UH17_52 RC {ECO:0000313|Proteomes:UP000031375}; RG RefSeq; RL Submitted (SEP-2015) to UniProtKB. CC -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. CC The N-terminal methionine is often cleaved when the second residue CC in the primary sequence is small and uncharged (Met-Ala-, Cys, CC Gly, Pro, Ser, Thr, or Val). Requires deformylation of the CC N(alpha)-formylated initiator methionine before it can be CC hydrolyzed. {ECO:0000256|HAMAP-Rule:MF_01974}. CC -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids, CC preferentially methionine, from peptides and arylamides. CC {ECO:0000256|HAMAP-Rule:MF_01974}. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01974}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01974}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01974}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01974}; 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}; 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- CC 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; CP010397; AJB66358.1; -; Genomic_DNA. DR EMBL; CP008706; AKA30982.1; -; Genomic_DNA. DR EMBL; CP010779; AKJ45008.1; -; Genomic_DNA. DR EMBL; CP012004; AKQ26271.1; -; Genomic_DNA. DR EMBL; AP014649; BAP65968.1; -; Genomic_DNA. DR EMBL; CVLE01000052; CQR67878.1; -; Genomic_DNA. DR EMBL; CVLF01000087; CQR89265.1; -; Genomic_DNA. DR EMBL; CVLD01000073; CRF38470.1; -; Genomic_DNA. DR EMBL; LN865143; CRL95227.1; -; Genomic_DNA. DR EMBL; LN868200; CRX64132.1; -; Genomic_DNA. DR EMBL; JRHB01000001; KGF60633.1; -; Genomic_DNA. DR EMBL; JWRT03000081; KHT74985.1; -; Genomic_DNA. DR EMBL; JWRU03000023; KHT85672.1; -; Genomic_DNA. DR EMBL; JWSF03000102; KHV18126.1; -; Genomic_DNA. DR EMBL; JWSE03000179; KHV22247.1; -; Genomic_DNA. DR EMBL; JWSH03000081; KHV28669.1; -; Genomic_DNA. DR EMBL; JWSI03000049; KHV33176.1; -; Genomic_DNA. DR EMBL; JWSJ03000006; KHV33855.1; -; Genomic_DNA. DR EMBL; JWUX03000152; KHX40556.1; -; Genomic_DNA. DR EMBL; JWYK03000081; KIA15515.1; -; Genomic_DNA. DR EMBL; JZIX02000006; KJE61738.1; -; Genomic_DNA. DR EMBL; JZIZ02000005; KJE63625.1; -; Genomic_DNA. DR EMBL; JZIY02000003; KJE68647.1; -; Genomic_DNA. DR EMBL; JZJA02000003; KJE73081.1; -; Genomic_DNA. DR EMBL; JZJB02000006; KJE74574.1; -; Genomic_DNA. DR EMBL; JZJE02000126; KJF02887.1; -; Genomic_DNA. DR EMBL; JZJD02000029; KJF05880.1; -; Genomic_DNA. DR EMBL; JZJF02000153; KJF11281.1; -; Genomic_DNA. DR EMBL; JZJG02000086; KJF15001.1; -; Genomic_DNA. DR EMBL; JWVA03000006; KJG75542.1; -; Genomic_DNA. DR EMBL; JWVC03000033; KJG77179.1; -; Genomic_DNA. DR EMBL; JWXB03000010; KJG81168.1; -; Genomic_DNA. DR EMBL; JZUF01000007; KKA96472.1; -; Genomic_DNA. DR EMBL; JZBX01000006; KKZ40688.1; -; Genomic_DNA. DR EMBL; JZCA01000048; KKZ44945.1; -; Genomic_DNA. DR EMBL; LFYX01000003; KMV03238.1; -; Genomic_DNA. DR EMBL; LFYZ01000001; KMV05062.1; -; Genomic_DNA. DR EMBL; LFYW01000001; KMV10717.1; -; Genomic_DNA. DR EMBL; LFYY01000001; KMV27219.1; -; Genomic_DNA. DR EMBL; LGYW01000003; KOP89520.1; -; Genomic_DNA. DR RefSeq; WP_001089491.1; NZ_LFYZ01000001.1. DR STRING; 575584.HMPREF0010_02353; -. DR EnsemblBacteria; AHB90780; AHB90780; P795_5275. DR EnsemblBacteria; AIA51932; AIA51932; BL01_08915. DR EnsemblBacteria; AIL76380; AIL76380; IX88_14615. DR EnsemblBacteria; AIL78573; AIL78573; IX87_07995. DR EnsemblBacteria; AIS07185; AIS07185; LX00_12565. DR EnsemblBacteria; AJB66358; AJB66358; RU84_05625. DR EnsemblBacteria; BAP65968; BAP65968; IOMTU433_1184. DR EnsemblBacteria; KEF45144; KEF45144; FL75_13250. DR EnsemblBacteria; KEF47159; KEF47159; FL80_16995. DR EnsemblBacteria; KFB64928; KFB64928; GQ86_18650. DR EnsemblBacteria; KFG14104; KFG14104; ABBL099_00550. DR EnsemblBacteria; KGF60633; KGF60633; LH92_12295. DR EnsemblBacteria; KHX40556; KHX40556; RQ85_11030. DR KEGG; abaa:IX88_14615; -. DR KEGG; abau:IX87_07995; -. DR KEGG; abk:LX00_12565; -. DR KEGG; abw:BL01_08915; -. DR eggNOG; ENOG4105CA1; Bacteria. DR eggNOG; COG0024; LUCA. DR KO; K01265; -. DR Proteomes; UP000028932; Chromosome. DR Proteomes; UP000031136; Chromosome. DR Proteomes; UP000031375; Unassembled WGS sequence. DR Proteomes; UP000031644; Chromosome. DR Proteomes; UP000032746; Chromosome. DR Proteomes; UP000033888; Unassembled WGS sequence. DR Proteomes; UP000034216; Unassembled WGS sequence. DR Proteomes; UP000035522; Chromosome. DR Proteomes; UP000036024; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.230.10; -; 1. DR HAMAP; MF_01974; MetAP_1; 1. DR InterPro; IPR001714; Pept_M24_MAP. DR InterPro; IPR000994; Pept_M24_structural-domain. 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:0000313|EMBL:KHX40556.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000028932, KW ECO:0000313|Proteomes:UP000031136}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000256|RuleBase:RU003652}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01974}. 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 //