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Database: UniProt
Entry: A0A1F8RUW6_9CHLR
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ID   A0A1F8RUW6_9CHLR        Unreviewed;       268 AA.
AC   A0A1F8RUW6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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   ORFNames=A2148_12075 {ECO:0000313|EMBL:OGO51465.1};
OS   Chloroflexi bacterium RBG_16_68_14.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797660 {ECO:0000313|EMBL:OGO51465.1, ECO:0000313|Proteomes:UP000176790};
RN   [1] {ECO:0000313|EMBL:OGO51465.1, ECO:0000313|Proteomes:UP000176790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGO51465.1}.
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DR   EMBL; MGOB01000051; OGO51465.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8RUW6; -.
DR   STRING; 1797660.A2148_12075; -.
DR   Proteomes; UP000176790; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003653};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974};
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          13..240
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         95
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         106
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         106
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         169
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         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         202
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         233
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         233
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"
SQ   SEQUENCE   268 AA;  29426 MW;  810BBA6EB119E0D6 CRC64;
     MPIIIKSDDE IAIMREAGRI VAEVLEILVA GVRPGLIVKK LDRIVQDQFE RRKVIPTFLG
     YLGYPARVCV SVNDEIVHGI PGDRVLREGD IVSIDLGATH KGFVADSALT VGVGRIRAEG
     QRLIDVTYQA LWEGIRAARP GARLGEISHA IQTCAEAHGY SVVREYVGHG VGREMHEEPQ
     VPNFGPPERG PILRKGMVLA LEPMVNIGDW RTKKHDDQWT VSTLDGSLSA HFEHTIAITD
     GEPEVLTLRS DEQPLLARTA ATAAERRS
//
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