(data stored in SCRATCH zone)

SWISSPROT: D5E8R3_METMS

ID   D5E8R3_METMS            Unreviewed;       296 AA.
AC   D5E8R3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 69.
DE   RecName: Full=Methionine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01975, ECO:0000256|RuleBase:RU003653};
DE            Short=MAP {ECO:0000256|HAMAP-Rule:MF_01975};
DE            Short=MetAP {ECO:0000256|HAMAP-Rule:MF_01975};
DE            EC=3.4.11.18 {ECO:0000256|HAMAP-Rule:MF_01975, ECO:0000256|RuleBase:RU003653};
DE   AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_01975};
GN   Name=map {ECO:0000256|HAMAP-Rule:MF_01975};
GN   OrderedLocusNames=Mmah_0034 {ECO:0000313|EMBL:ADE35572.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35572.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35572.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000256|HAMAP-Rule:MF_01975,
CC       ECO:0000256|RuleBase:RU003653}.
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_01975,
CC         ECO:0000256|RuleBase:RU003653};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01975,
CC         ECO:0000256|RuleBase:RU003653};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01975,
CC         ECO:0000256|RuleBase:RU003653};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01975,
CC         ECO:0000256|RuleBase:RU003653};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01975,
CC         ECO:0000256|RuleBase:RU003653};
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_01975, ECO:0000256|RuleBase:RU003653};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01975}.
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase archaeal type 2 subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01975}.
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DR   EMBL; CP001994; ADE35572.1; -; Genomic_DNA.
DR   RefSeq; WP_013036515.1; NC_014002.1.
DR   MEROPS; M24.035; -.
DR   EnsemblBacteria; ADE35572; ADE35572; Mmah_0034.
DR   GeneID; 8982165; -.
DR   KEGG; mmh:Mmah_0034; -.
DR   eggNOG; arCOG01001; Archaea.
DR   eggNOG; COG0024; LUCA.
DR   HOGENOM; HOG000226277; -.
DR   KO; K01265; -.
DR   OMA; NEIAAHY; -.
DR   OrthoDB; 82853at2157; -.
DR   BioCyc; MMAH547558:G1GHT-34-MONOMER; -.
DR   Proteomes; UP000001059; 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; cd01088; MetAP2; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   HAMAP; MF_01975; MetAP_2_arc; 1.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR028595; MetAP_archaeal.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001714; Pept_M24_MAP.
DR   InterPro; IPR002468; Pept_M24A_MAP2.
DR   InterPro; IPR018349; Pept_M24A_MAP2_BS.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   TIGRFAMs; TIGR00501; met_pdase_II; 1.
DR   PROSITE; PS01202; MAP_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E8R3.
DR   SWISS-2DPAGE; D5E8R3.
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01975,
KW   ECO:0000256|RuleBase:RU003653, ECO:0000313|EMBL:ADE35572.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01975, ECO:0000313|EMBL:ADE35572.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01975,
KW   ECO:0000256|RuleBase:RU003653};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01975, ECO:0000256|RuleBase:RU003653};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN          14..288
FT                   /note="Peptidase_M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   METAL           90
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01975"
FT   METAL           101
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01975"
FT   METAL           101
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01975"
FT   METAL           160
FT                   /note="Divalent metal cation 2; catalytic; via tele
FT                   nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01975"
FT   METAL           193
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01975"
FT   METAL           281
FT                   /note="Divalent metal cation 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01975"
FT   METAL           281
FT                   /note="Divalent metal cation 2; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01975"
FT   BINDING         71
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01975"
FT   BINDING         168
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01975"
SQ   SEQUENCE   296 AA;  32017 MW;  C698B6B04DB01441 CRC64;
     MQDKFQEVED ILDKYLTAGK ILSQVRGEAA DKIRVGAKLL DVAEFVEQRT MELGGKPAFP
     CNLSRNDEAA HATPTAGDTT VFGKDIVKLD MGVHVDGYIA DAALTVDLSG NKDLVDASRQ
     ALEAAIDTVK GGVNTAEIGA VIEDTIRDKG FKPVANLTGH GLARYQAHTP PSIPNRHIGE
     GMELQAGDII AIEPFATDGA GKISDGSFTE IYQFIQKKPI RMPAARKLLK ELKEYSTLPF
     AKRWLTSPKI DLALMQLEKA EIITSFPVLK EVGGGMVSQA EHTLIVTEDG CEITTR
//

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