(data stored in SCRATCH zone)

SWISSPROT: C8W406_DESAS

ID   C8W406_DESAS            Unreviewed;       249 AA.
AC   C8W406;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 69.
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   OrderedLocusNames=Dtox_0307 {ECO:0000313|EMBL:ACV61260.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61260.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61260.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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:
CC       Reaction=Release of N-terminal amino acids, preferentially
CC         methionine, 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; 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   -!- 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; CP001720; ACV61260.1; -; Genomic_DNA.
DR   RefSeq; WP_015755981.1; NC_013216.1.
DR   STRING; 485916.Dtox_0307; -.
DR   EnsemblBacteria; ACV61260; ACV61260; Dtox_0307.
DR   KEGG; dae:Dtox_0307; -.
DR   eggNOG; ENOG4105CA1; Bacteria.
DR   eggNOG; COG0024; LUCA.
DR   HOGENOM; HOG000030426; -.
DR   KO; K01265; -.
DR   OMA; SYFHGPP; -.
DR   OrthoDB; 1285136at2; -.
DR   BioCyc; DACE485916:G1GFV-322-MONOMER; -.
DR   Proteomes; UP000002217; 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;
DR   PRODOM; C8W406.
DR   SWISS-2DPAGE; C8W406.
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974,
KW   ECO:0000256|RuleBase:RU003653, ECO:0000313|EMBL:ACV61260.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
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,
KW   ECO:0000256|RuleBase:RU003653};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN       13    239       Peptidase_M24. {ECO:0000259|Pfam:
FT                                PF00557}.
FT   METAL        94     94       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       105    105       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       105    105       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       168    168       Divalent metal cation 2; catalytic; via
FT                                tele nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01974}.
FT   METAL       201    201       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       232    232       Divalent metal cation 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   METAL       232    232       Divalent metal cation 2; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01974}.
FT   BINDING      77     77       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01974}.
FT   BINDING     175    175       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01974}.
SQ   SEQUENCE   249 AA;  27274 MW;  5E8C3F387FBF9393 CRC64;
     MITCKSEREL MYMREAGKIA AEALAKLAGA VQPGVTTKEL DRLAEEYIRS CGARPAFKGL
     YGFPATICSS VNEEVVHGIP GLRKLENGDI ISIDIGTEVN GYFGDCAVTL AVGKVSDEAW
     RLIKVTEESF YAGIAKAKIG NRLSDISNAV QKYVEEHGFS VVRDYVGHGI GSSMHEEPQV
     PNFGKPGRGP RLQAGMTLAI EPMVNMGTYE VRTLPDNWTV VTKDRKLSSH YEHTIAITDN
     EPEILTRLK
//

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