(data stored in ACNUC7421 zone)

SWISSPROT: C8VVA6_DESAS

ID   C8VVA6_DESAS            Unreviewed;       427 AA.
AC   C8VVA6;
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=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   OrderedLocusNames=Dtox_0010 {ECO:0000313|EMBL:ACV60975.1};
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:ACV60975.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV60975.1, 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: 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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00011};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00011};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP 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; CP001720; ACV60975.1; -; Genomic_DNA.
DR   RefSeq; WP_012813427.1; NC_013216.1.
DR   STRING; 485916.Dtox_0010; -.
DR   EnsemblBacteria; ACV60975; ACV60975; Dtox_0010.
DR   KEGG; dae:Dtox_0010; -.
DR   eggNOG; ENOG4105C91; Bacteria.
DR   eggNOG; COG0104; LUCA.
DR   HOGENOM; HOG000260959; -.
DR   KO; K01939; -.
DR   OMA; SNAGHTV; -.
DR   OrthoDB; 232152at2; -.
DR   BioCyc; DACE485916:G1GFV-10-MONOMER; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000002217; 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; 1.10.300.10; -; 1.
DR   Gene3D; 3.40.440.10; -; 1.
DR   Gene3D; 3.90.170.10; -; 1.
DR   HAMAP; MF_00011; Adenylosucc_synth; 1.
DR   InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR   InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
DR   InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR   InterPro; IPR042110; Adenylosuccinate_synth_dom2.
DR   InterPro; IPR042111; Adenylosuccinate_synth_dom3.
DR   InterPro; IPR001114; Adenylosuccinate_synthetase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11846; PTHR11846; 1.
DR   Pfam; PF00709; Adenylsucc_synt; 1.
DR   SMART; SM00788; Adenylsucc_synt; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00184; purA; 1.
DR   PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR   PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8VVA6.
DR   SWISS-2DPAGE; C8VVA6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
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,
KW   ECO:0000256|RuleBase:RU000520, ECO:0000313|EMBL:ACV60975.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00011,
KW   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:UP000002217}.
FT   NP_BIND      12     18       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   NP_BIND      40     42       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   NP_BIND     330    332       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   NP_BIND     412    414       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   REGION       13     16       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   REGION       38     41       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   REGION      298    304       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00011}.
FT   ACT_SITE     13     13       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   ACT_SITE     41     41       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   ACT_SITE    139    139       {ECO:0000256|PROSITE-ProRule:PRU10134}.
FT   METAL        13     13       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   METAL        40     40       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     128    128       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     142    142       IMP; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     223    223       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     238    238       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     302    302       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     304    304       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
SQ   SEQUENCE   427 AA;  47458 MW;  950DEE5479642866 CRC64;
     MSTVVLIGAQ WGDEGKGKVT DYLSERADMV VRYQGGNNAG HTVVVGDDEF KLHLIPSGIL
     YKDKLCLIGN GVVIDPSVLM EEIKGLQERG INTDNLRIST RAHVILPYHR ELDKAEEDSK
     GKNKIGTTCR GIGPTYMDKS ARVGVRIIDL MEEDRLAEIL EMNIKTKNKI LTKVYDHESF
     NFNEVFKIAK QYADNLRKYV TDTSLLINDV IDEGKNVLFE GAQGTLLDLD HGTYPYVTSS
     NPVAAGACLG AGVGPTKINK ILGVVKAYTT RVGEGPFLTE LMDNLGEMIR QNGREFGTTT
     GRPRRCGWYD AVITRYAVRI NGLTFLAVTK LDVLTGLEKL KICTGYKFED KILKDFPCSL
     KTLTKCEPVY EEMPGWQEDI SQIKNFADLP VNAQRYLNRI AELAGVPVAV IGVGMKRDQT
     IIVHELF
//

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