(data stored in ACNUC7421 zone)

SWISSPROT: D4YXD3_SPHJU

ID   D4YXD3_SPHJU            Unreviewed;       429 AA.
AC   D4YXD3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 50.
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:BAI95015.1};
GN   OrderedLocusNames=SJA_C1-01810 {ECO:0000313|EMBL:BAI95015.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95015.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95015.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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: GTP + IMP + L-aspartate = GDP + phosphate +
CC       N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000256|HAMAP-Rule:MF_00011,
CC       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; AP010803; BAI95015.1; -; Genomic_DNA.
DR   RefSeq; WP_007685463.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-01810; -.
DR   EnsemblBacteria; BAI95015; BAI95015; SJA_C1-01810.
DR   GeneID; 29271887; -.
DR   KEGG; sjp:SJA_C1-01810; -.
DR   eggNOG; ENOG4105C91; Bacteria.
DR   eggNOG; COG0104; LUCA.
DR   HOGENOM; HOG000260959; -.
DR   KO; K01939; -.
DR   OMA; GVSKAYT; -.
DR   OrthoDB; POG091H01G9; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03108; AdSS; 1.
DR   HAMAP; MF_00011; Adenylosucc_synth; 1.
DR   InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR   InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
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; D4YXD3.
DR   SWISS-2DPAGE; D4YXD3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
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:BAI95015.1};
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:UP000007753}.
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    140    140       {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     129    129       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     143    143       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   429 AA;  46373 MW;  58A7C9D1AD49E136 CRC64;
     MANVTVIGAQ WGDEGKGKIV DWLSERADVV ARFQGGHNAG HTLVVGEKVY KLSLLPSGIV
     RGTLSVIGNG VVLDPWHFRD EVAKLKGQGV EITPDNLQIA ETCPLILPFH RDLDGLREDA
     SGAGKIGTTR RGIGPAYEDK VGRRAIRVCD LAHLDDLGPQ LDRLTAHHDA LRAGFNEAPI
     DRDALMAELR DIAGFILPFV KPVWLTLNKA KAEGKRILFE GAQGTLLDID HGTYPFVTSS
     NTVAGTAASG TGLGPNGAGF VLGIVKAYTT RVGSGPFPTE QENDVGQRLG ERGHEFGTVT
     GRKRRCGWFD AVLVRQSVAV SGVTGIALTK LDVLDGFDEL KICVGYRIGD RHFDYLPAHA
     QDQAKAEPVY ESIEGWQDTT AGARSWAELP AQAIKYIRRI EELIGCPVTL VSTSPEREDT
     ILVRDPFAD
//

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