PUR72_CAUVC
ID PUR72_CAUVC Reviewed; 320 AA.
AC Q9A3G2;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Putative phosphoribosylaminoimidazole-succinocarboxamide synthase 2;
DE EC=6.3.2.6;
DE AltName: Full=SAICAR synthetase 2;
GN Name=purC2; OrderedLocusNames=CC_3242;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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; AE005673; AAK25204.1; -; Genomic_DNA.
DR PIR; H87650; H87650.
DR RefSeq; NP_422036.1; NC_002696.2.
DR RefSeq; WP_010921075.1; NC_002696.2.
DR AlphaFoldDB; Q9A3G2; -.
DR SMR; Q9A3G2; -.
DR STRING; 190650.CC_3242; -.
DR EnsemblBacteria; AAK25204; AAK25204; CC_3242.
DR KEGG; ccr:CC_3242; -.
DR PATRIC; fig|190650.5.peg.3247; -.
DR eggNOG; COG0152; Bacteria.
DR HOGENOM; CLU_045637_0_1_5; -.
DR OMA; TKFEFGF; -.
DR BioCyc; CAULO:CC3242-MON; -.
DR UniPathway; UPA00074; UER00131.
DR Proteomes; UP000001816; 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 HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR Pfam; PF01259; SAICAR_synt; 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;
KW Reference proteome.
FT CHAIN 1..320
FT /note="Putative phosphoribosylaminoimidazole-
FT succinocarboxamide synthase 2"
FT /id="PRO_0000100814"
SQ SEQUENCE 320 AA; 34930 MW; 9DDF4098C98AB4C3 CRC64;
MTLSAPNALA VVDLPCLPNH YRGKVRDNYD LPDGRRVIVA SDRLSAFDRN LCAVPGKGQV
LTETARFWFD ATADICPNHV VAYPDPNVLI GKRLKMLPVE LVVRGYLAGT TSTSILTLYN
KGERQMYGVT LPDGLKANQR LPQAILTPTS KAADGDHDAP LSPDEVLAQG LVTPAQWEQL
SAYALALFAR GQAMAAERGL ILADTKYEFG LDETGAIVLA DEIHTPDSSR FWKAATYEAR
FEAGQRPESF DKDFVRAWVA ERCDPYNDSI PEIPAELIAQ ASAVYIEAFE AITGQTFAAP
DASEPVMARV KRNLDAYLAG