(data stored in ACNUC7421 zone)

SWISSPROT: C7PX97_CATAD

ID   C7PX97_CATAD            Unreviewed;       550 AA.
AC   C7PX97;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 61.
DE   RecName: Full=Adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_00011};
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};
DE   AltName: Full=IMP--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_00011};
GN   Name=purA {ECO:0000256|HAMAP-Rule:MF_00011};
GN   OrderedLocusNames=Caci_0498 {ECO:0000313|EMBL:ACU69448.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69448.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69448.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(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: GTP + IMP + L-aspartate = GDP + phosphate +
CC       N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
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   -!- 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00011}.
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DR   EMBL; CP001700; ACU69448.1; -; Genomic_DNA.
DR   RefSeq; WP_012784743.1; NC_013131.1.
DR   ProteinModelPortal; C7PX97; -.
DR   STRING; 479433.Caci_0498; -.
DR   EnsemblBacteria; ACU69448; ACU69448; Caci_0498.
DR   KEGG; cai:Caci_0498; -.
DR   eggNOG; ENOG4106ISN; Bacteria.
DR   eggNOG; COG0104; LUCA.
DR   HOGENOM; HOG000115995; -.
DR   KO; K01939; -.
DR   OMA; RTYPIRV; -.
DR   OrthoDB; POG091H1KDP; -.
DR   UniPathway; UPA00075; UER00335.
DR   Proteomes; UP000000851; Chromosome.
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   HAMAP; MF_00011; Adenylosucc_synth; 1.
DR   InterPro; IPR001114; Adenylosuccinate_synthetase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11846; PTHR11846; 1.
DR   Pfam; PF00709; Adenylsucc_synt; 2.
DR   SMART; SM00788; Adenylsucc_synt; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
PE   3: Inferred from homology;
DR   PRODOM; C7PX97.
DR   SWISS-2DPAGE; C7PX97.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00011};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00011};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000313|EMBL:ACU69448.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00011};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00011};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00011};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT   NP_BIND     236    238       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   NP_BIND     496    498       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   REGION      234    237       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   ACT_SITE    237    237       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00011}.
FT   METAL       236    236       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     316    316       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     377    377       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     392    392       IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.
FT   BINDING     470    470       GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.
SQ   SEQUENCE   550 AA;  60177 MW;  33A9FCA7AE1E547E CRC64;
     MKTRPRLVVI SGPVGSGKST LARRLVSRYG AFDIRTQDLM RAHAVAYDKE LPLERRALQE
     YGEQLDIDTG GGWVAEGVAK LLDQRDEPID GHGLIVVDSV RAHHQVERLR EAYGARVTHI
     HLNAPESVLG ERYAERGDAS GLVELDSYTE VAQNKTESAV GQLESEADIT IDTQRNLPGD
     VETRAAAALG LYASRTDKLV DVLIGAQYGS EGKGNIAFYL APEYDVLVRV GGPNAGHKVP
     LPTPYTHRLL PSGSRANLAA CIVIGPGATL SLEVLMREIA ESGVEVDRLS IDPQCMIIEN
     ADLDAEAQLV GKIGSTGKGG GAAAARRIMG RHYDEASETP VRLARDVQEL VPYVRPTGEI
     LDDAFARGHR VLLEGTQGTG LSLYHGSYPH VTSRDTTTAG TLAEAGIGIH RVRRVIIVAR
     TYPIRVKNPD EGTSGPMSQE LSWEEIARRS GIPEEELVKQ EKGSVSNNQR RVAEFDWQML
     RRASEINGAT DVALTFTDYL DIGNRDARRY EQLSPKTIDF IEEVERVAGV PVSLLGTRFD
     IRSVIDRRQW
//

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