(data stored in ACNUC30630 zone)

SWISSPROT: PUR7_TROW8

ID   PUR7_TROW8              Reviewed;         305 AA.
AC   Q83IB9;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   11-DEC-2019, entry version 93.
DE   RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase {ECO:0000255|HAMAP-Rule:MF_00137};
DE            EC=6.3.2.6 {ECO:0000255|HAMAP-Rule:MF_00137};
DE   AltName: Full=SAICAR synthetase {ECO:0000255|HAMAP-Rule:MF_00137};
GN   Name=purC {ECO:0000255|HAMAP-Rule:MF_00137}; OrderedLocusNames=TW119;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP +
CC         L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-
CC         4-carboxamido]succinate + ADP + 2 H(+) + phosphate;
CC         Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58443,
CC         ChEBI:CHEBI:77657, ChEBI:CHEBI:456216; EC=6.3.2.6;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00137};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC       phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC       {ECO:0000255|HAMAP-Rule:MF_00137}.
CC   -!- SIMILARITY: Belongs to the SAICAR synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00137}.
DR   EMBL; BX251410; CAD66801.1; -; Genomic_DNA.
DR   RefSeq; WP_011096082.1; NC_004551.1.
DR   SMR; Q83IB9; -.
DR   EnsemblBacteria; CAD66801; CAD66801; TW119.
DR   KEGG; tws:TW119; -.
DR   HOGENOM; HOG000230360; -.
DR   KO; K01923; -.
DR   OMA; CEPFKVE; -.
DR   BioCyc; GCF_000196075:G1EE9-125-MONOMER; -.
DR   UniPathway; UPA00074; UER00131.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00137; SAICAR_synth; 1.
DR   InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR   InterPro; IPR018236; SAICAR_synthetase_CS.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR   PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q83IB9.
DR   SWISS-2DPAGE; Q83IB9.
KW   ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..305
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase"
FT                   /id="PRO_0000100893"
SQ   SEQUENCE   305 AA;  35415 MW;  59BDFD8C0AB4790A CRC64;
     MTRKLEIPES RDLPDWSHIG GGKVRELYVH RQYKNILLMF ASNRVSAFDF VLEPEIPEKG
     RMLTQMSNWW FRKLPAENHL LENYDQELYR DLASHIPSHI LERSTICRKM DIIPFEFVIR
     GYLTGSAWAD YLENNTVYGI KLKGKFRQGD RLPGPIFTPT TKSRTKDTPV RYEDLVNAIG
     LSHAQQLREM CTDYYTTAEQ IARNKGLIIA DAKFEFGIAE GKAYLADELL TADSARYWDI
     NSWGQFDLPI ERRLDSFDKQ AVRDWVKCNS GKNITPQNIT PLRLPQELIQ TVYKKYKTLL
     AKLTG
//

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