PUR7_BRUC2
ID PUR7_BRUC2 Reviewed; 254 AA.
AC A9MAL9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=BCAN_A0857;
OS Brucella canis (strain ATCC 23365 / NCTC 10854).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=483179;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23365 / NCTC 10854;
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000872; ABX61922.1; -; Genomic_DNA.
DR RefSeq; WP_004688254.1; NC_010103.1.
DR AlphaFoldDB; A9MAL9; -.
DR SMR; A9MAL9; -.
DR EnsemblBacteria; ABX61922; ABX61922; BCAN_A0857.
DR GeneID; 45124272; -.
DR GeneID; 57306936; -.
DR KEGG; bcs:BCAN_A0857; -.
DR HOGENOM; CLU_061495_2_0_5; -.
DR OMA; EFCYKND; -.
DR PhylomeDB; A9MAL9; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000001385; Chromosome I.
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..254
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_1000076446"
SQ SEQUENCE 254 AA; 28956 MW; B4084597AFDE39A5 CRC64;
MNRRRRIYEG KAKILYEGPE PGTLVQFFKD DATAFNAKKH EVIDGKGVLN NRISEHIFTQ
LNRIGIPTHF IRRLNMREQL IKEVEIIPLE VVVRNVAAGS LAKRLGLEEG TILPRSIIEF
YYKADALDDP MVTEEHITAF GWASPQEIDD IMALAIRVND FLTGLFLGIG IQLVDFKMEC
GRLWEGDMMR IVVADEISPD SARLWDITTN DKLDKDRFRR DMGGLVEAYQ EVARRLGIMN
ENDTPRPSGP TLVK
