(data stored in ACNUC10043 zone)

SWISSPROT: D1YV79_METPS

ID   D1YV79_METPS            Unreviewed;       337 AA.
AC   D1YV79;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 67.
DE   RecName: Full=Adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
DE            Short=AMPSase {ECO:0000256|HAMAP-Rule:MF_00011};
DE            Short=AdSS {ECO:0000256|HAMAP-Rule:MF_00011};
DE            EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
DE   AltName: Full=IMP--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_00011};
GN   Name=purA {ECO:0000256|HAMAP-Rule:MF_00011,
GN   ECO:0000313|EMBL:BAI60351.1};
GN   OrderedLocusNames=MCP_0279 {ECO:0000313|EMBL:BAI60351.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60351.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Plays an important role in the de novo pathway of purine
CC       nucleotide biosynthesis. Catalyzes the first committed step in the
CC       biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-
CC         dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053,
CC         ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00011};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00011};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC       from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00011,
CC       ECO:0000256|RuleBase:RU000520}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00011}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011}.
CC   -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520}.
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DR   EMBL; AP011532; BAI60351.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0279; -.
DR   EnsemblBacteria; BAI60351; BAI60351; MCP_0279.
DR   KEGG; mpd:MCP_0279; -.
DR   PATRIC; fig|304371.9.peg.283; -.
DR   eggNOG; arCOG04387; Archaea.
DR   eggNOG; COG0104; LUCA.
DR   HOGENOM; HOG000260959; -.
DR   KO; K01939; -.
DR   OMA; FHHAKPI; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03108; AdSS; 1.
DR   Gene3D; 3.40.440.10; -; 1.
DR   HAMAP; MF_00011; Adenylosucc_synth; 1.
DR   InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR   InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR   InterPro; IPR001114; Adenylosuccinate_synthetase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11846; PTHR11846; 2.
DR   Pfam; PF00709; Adenylsucc_synt; 2.
DR   SMART; SM00788; Adenylsucc_synt; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YV79.
DR   SWISS-2DPAGE; D1YV79.
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00011,
KW   ECO:0000256|RuleBase:RU000520};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882}.
FT   NP_BIND         12..18
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   NP_BIND         42..44
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   NP_BIND         281..283
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   NP_BIND         321..323
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   REGION          13..16
FT                   /note="IMP binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   REGION          40..43
FT                   /note="IMP binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   REGION          249..255
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   ACT_SITE        13
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   ACT_SITE        43
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   METAL           13
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   METAL           42
FT                   /note="Magnesium; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   BINDING         124
FT                   /note="IMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   BINDING         138
FT                   /note="IMP; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   BINDING         176
FT                   /note="IMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   BINDING         191
FT                   /note="IMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   BINDING         253
FT                   /note="IMP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
FT   BINDING         255
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00011"
SQ   SEQUENCE   337 AA;  36267 MW;  7DE9691B590CD532 CRC64;
     MVSTIVVGGF FGDEGKGKIV AHIAYTEHPS IIARGGVGPN AGHTVYKDGV KYGVRMVPSG
     FVYDKARLLI GAGVLVDPVV LDREVKLLGC GGRIGVDYRC SIIEEKHIAE DKGTERLAKK
     IGTTGTGCGP ANKERVMRSA KQAADVESLK KYLTDVSQEC NDALDRGENL IIEGSQGFGI
     SLYYGTYPFV TSKDTSASSL AADVGVGPTK IDEVVVVFKA FPTRVGEGPF ETEMTPEEAQ
     KRGIAEFGTV TGRARRIGYW DPKMARYSAM INGATQAAIT GLDRIDPAVK GVQEYDKLTE
     NVKEFVKQAE KDAGVPFTLL STGPDQKDIV DLRNHKK
//

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