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PUR7_PYRAB
ID   PUR7_PYRAB              Reviewed;         234 AA.
AC   Q9V254; G8ZG55;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 3.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase;
DE            EC=6.3.2.6;
DE   AltName: Full=SAICAR synthetase;
GN   Name=purC; OrderedLocusNames=PYRAB02200; ORFNames=PAB2400;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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   -!- 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   -!- SIMILARITY: Belongs to the SAICAR synthetase family. {ECO:0000305}.
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DR   EMBL; AJ248283; CAB49144.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69596.1; -; Genomic_DNA.
DR   PIR; A75212; A75212.
DR   RefSeq; WP_010867344.1; NC_000868.1.
DR   AlphaFoldDB; Q9V254; -.
DR   SMR; Q9V254; -.
DR   STRING; 272844.PAB2400; -.
DR   EnsemblBacteria; CAB49144; CAB49144; PAB2400.
DR   GeneID; 1495109; -.
DR   KEGG; pab:PAB2400; -.
DR   PATRIC; fig|272844.11.peg.236; -.
DR   eggNOG; arCOG04421; Archaea.
DR   HOGENOM; CLU_061495_2_0_2; -.
DR   OrthoDB; 47738at2157; -.
DR   UniPathway; UPA00074; UER00131.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
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   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR   CDD; cd01415; SAICAR_synt_PurC; 1.
DR   HAMAP; MF_00137; SAICAR_synth; 1.
DR   InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR   InterPro; IPR033934; SAICAR_synt_PurC.
DR   InterPro; IPR001636; SAICAR_synth.
DR   InterPro; IPR018236; SAICAR_synthetase_CS.
DR   Pfam; PF01259; SAICAR_synt; 1.
DR   TIGRFAMs; TIGR00081; purC; 1.
DR   PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
DR   PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT   CHAIN           1..234
FT                   /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT                   synthase"
FT                   /id="PRO_0000100913"
SQ   SEQUENCE   234 AA;  26974 MW;  87FF6C1C5B6B458A CRC64;
     MEVYEGKAKK MIPMDDDKFI MEFKDDATAF DGVKKAKFKG KGWLNAQISA KFFKLLEEHG
     IKTHFIGVAG DNKLIVEKLD MYPLEVVVRN VVAGSLKKRL PLPEGYELPE PIVELYYKSD
     ELHDPMINYY HAKILGITLE EIKKMEEIAL KVNEILKDYL AKRGIILVDF KLEFGKNKNG
     EIILADEISP DTCRFWDAET KKSLDKDVFR FDKGDLIEAY EELYRRITGE DPGN
 
 
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