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}.
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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
//