PUR7_WOLWR
ID PUR7_WOLWR Reviewed; 240 AA.
AC C0R444;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 73.
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=WRi_009790;
OS Wolbachia sp. subsp. Drosophila simulans (strain wRi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia; unclassified Wolbachia.
OX NCBI_TaxID=66084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wRi;
RX PubMed=19307581; DOI=10.1073/pnas.0810753106;
RA Klasson L., Westberg J., Sapountzis P., Naeslund K., Lutnaes Y.,
RA Darby A.C., Veneti Z., Chen L., Braig H.R., Garrett R., Bourtzis K.,
RA Andersson S.G.;
RT "The mosaic genome structure of the Wolbachia wRi strain infecting
RT Drosophila simulans.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5725-5730(2009).
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; CP001391; ACN95686.1; -; Genomic_DNA.
DR RefSeq; WP_007549278.1; NZ_MKIF01000073.1.
DR AlphaFoldDB; C0R444; -.
DR SMR; C0R444; -.
DR STRING; 66084.WRi_009790; -.
DR EnsemblBacteria; ACN95686; ACN95686; WRi_009790.
DR KEGG; wri:WRi_009790; -.
DR HOGENOM; CLU_061495_2_0_5; -.
DR OMA; EFCYKND; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000001293; 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..240
FT /note="Phosphoribosylaminoimidazole-succinocarboxamide
FT synthase"
FT /id="PRO_1000122940"
SQ SEQUENCE 240 AA; 27681 MW; A2FC419788AB44FD CRC64;
MSLNKTIYEG KAKAIIETED SSTVIQHFKD DVTAFNKEKY EIIESKGIIN NHISAFIMEK
LEKAEISTHF IKTLNEREQL VKKLKIIPLE VVVRNVAAGS FCKRFNIKEG ERLASPIIDF
FYKNDDLADP MVSENHILYF DWLSSKEMDE VKTTTLKINE ILVHLFSNAS IYLVDLKLEF
GRLINDSTKI VLADEISPDN CRLWDKNTYK KLDKDVFRLN LGDLKEAYLE VAKRLSVKLG
