PUR7_METS3
ID PUR7_METS3 Reviewed; 243 AA.
AC A5UNH4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
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=Msm_1547;
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000678; ABQ87752.1; -; Genomic_DNA.
DR RefSeq; WP_004035282.1; NC_009515.1.
DR AlphaFoldDB; A5UNH4; -.
DR SMR; A5UNH4; -.
DR STRING; 420247.Msm_1547; -.
DR EnsemblBacteria; ABQ87752; ABQ87752; Msm_1547.
DR GeneID; 5216568; -.
DR KEGG; msi:Msm_1547; -.
DR PATRIC; fig|420247.28.peg.1538; -.
DR eggNOG; arCOG04421; Archaea.
DR HOGENOM; CLU_061495_2_0_2; -.
DR OMA; EFCYKND; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000001992; 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.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..243
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_1000018733"
SQ SEQUENCE 243 AA; 27492 MW; 15204DF8376E3A86 CRC64;
MDKKELINNG KVKSVYTTDD ENAVIIEFRD DMTAGDGARK EVMNKKGSYN ALISTKLFKV
LEENGIKTQF IDLPETNVMV AKKLEMIPIE VIVRNIATGS LIRKYPIADG TKLDPPIVQM
DFKADEFHDP MLNDSIIKAL GLATQEEIDE LTEKALKINE VLSEFLLEAG IILVDFKVEF
GKDKNGEIIL GDEISPDGCR LWDSETLDML DKELFRKGKD NEVMDAYVEV YNRIIPDDEK
IEL
