MAP1_MYCGA
ID MAP1_MYCGA Reviewed; 250 AA.
AC O52353;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Methionine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_01974};
DE Short=MAP {ECO:0000255|HAMAP-Rule:MF_01974};
DE Short=MetAP {ECO:0000255|HAMAP-Rule:MF_01974};
DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_01974};
DE AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_01974};
GN Name=map {ECO:0000255|HAMAP-Rule:MF_01974}; OrderedLocusNames=MYCGA0720;
GN ORFNames=MGA_0745;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A5969Var.B;
RX PubMed=10867916;
RA Skamrov A.V., Gol'dman M.A., Feoktistova E.S., Bibilashvili R.S.;
RT "Determination and analysis of the nucleotide sequence of a segment of a
RT Mycoplasma gallisepticum strain A5969 chromosome, containing operons S10
RT and rrn23-5.";
RL Mol. Biol. (Mosk.) 34:390-396(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
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. {ECO:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_01974};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01974};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01974};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01974}.
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01974}.
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DR EMBL; AF036708; AAB95408.1; -; Genomic_DNA.
DR EMBL; AE015450; AAP56422.1; -; Genomic_DNA.
DR RefSeq; WP_011113301.1; NC_004829.2.
DR AlphaFoldDB; O52353; -.
DR SMR; O52353; -.
DR KEGG; mga:MGA_0745; -.
DR PATRIC; fig|233150.7.peg.76; -.
DR HOGENOM; CLU_015857_0_1_14; -.
DR OMA; GDHAYTF; -.
DR OrthoDB; 1285136at2; -.
DR Proteomes; UP000001418; Chromosome.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046914; F:transition metal ion binding; IEA:UniProt.
DR GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01086; MetAP1; 1.
DR Gene3D; 3.90.230.10; -; 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; Hydrolase; Metal-binding; Protease; Reference proteome.
FT CHAIN 1..250
FT /note="Methionine aminopeptidase"
FT /id="PRO_0000148945"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT BINDING 94
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT BINDING 105
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT BINDING 105
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_01974"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_01974"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT BINDING 235
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974"
FT CONFLICT 73
FT /note="Q -> K (in Ref. 1; AAB95408)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="E -> D (in Ref. 1; AAB95408)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="P -> L (in Ref. 1; AAB95408)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="E -> D (in Ref. 1; AAB95408)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="Y -> H (in Ref. 1; AAB95408)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="S -> N (in Ref. 1; AAB95408)"
FT /evidence="ECO:0000305"
FT CONFLICT 189..190
FT /note="SS -> PG (in Ref. 1; AAB95408)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="D -> V (in Ref. 1; AAB95408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 250 AA; 29026 MW; F7EE9B91D4779F76 CRC64;
MIYIKNPNEI QKIKNAAQIY KKIVKQFNFD YIKNKSLKEI DQMLRDFVSQ HHANSCYHGY
LGFKGYHCLS LNQTIIHGLA NDEIFTSKDK LTIDIGIELD NYYCDSAFTI LGPDVNPRQK
LLSEVTHNCI FELVKKIVPN QTTTNDLGIW TEEYAKKYGY SVIKDFGGHG CGIKIHEDPI
ILNYGTKKSS ELLTPNMVIC IEPMFFEKDN RYYIDPDDSW SVKPVNKNQY VCHWEHMVLI
KEDQAEILTL
