PUR7_BARQU
ID PUR7_BARQU Reviewed; 254 AA.
AC Q6FZJ2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=BQ07470;
OS Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Toulouse;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897700; CAF26231.1; -; Genomic_DNA.
DR RefSeq; WP_011179483.1; NC_005955.1.
DR AlphaFoldDB; Q6FZJ2; -.
DR SMR; Q6FZJ2; -.
DR STRING; 283165.BQ07470; -.
DR EnsemblBacteria; CAF26231; CAF26231; BQ07470.
DR KEGG; bqu:BQ07470; -.
DR eggNOG; COG0152; Bacteria.
DR HOGENOM; CLU_061495_2_0_5; -.
DR OMA; EFCYKND; -.
DR OrthoDB; 1345271at2; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000000597; 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..254
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_1000018672"
SQ SEQUENCE 254 AA; 29125 MW; 3BA3C37E0042094B CRC64;
MNRRHRIYEG KAKILYEGPE PGTYIQFFKD DATAFNAKKH EVIDGKGVLN NRISEHIFSH
LGRLGIPTHF IKRINMREQL IKAVEIIPLE VVVRNVAAGS LSKRLGLEEG TVLSQSIIEF
YYKNDSLDDP MVTEEHITAF GWAVPQEIED IMQLSIRIND FLSGLFAAAN IQLIDFKMEF
GRLWEDEAMR IVLADEISPD SARLWDMQTR EKMDKDRFRR NMGGLINAYQ EVAKRLGIIN
ENEPPRPSGP VLVK