NADC_RHORU
ID NADC_RHORU Reviewed; 296 AA.
AC P77938;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Probable nicotinate-nucleotide pyrophosphorylase [carboxylating];
DE EC=2.4.2.19;
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating];
DE Short=QAPRTase;
GN Name=nadC;
OS Rhodospirillum rubrum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=1085;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UR1;
RX PubMed=7721706; DOI=10.1128/jb.177.8.2157-2163.1995;
RA Shelver D., Kerby R.L., He Y., Roberts G.P.;
RT "Carbon monoxide-induced activation of gene expression in Rhodospirillum
RT rubrum requires the product of cooA, a member of the cyclic AMP receptor
RT protein family of transcriptional regulators.";
RL J. Bacteriol. 177:2157-2163(1995).
CC -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CO2 + diphosphate + nicotinate beta-D-ribonucleotide = 5-
CC phospho-alpha-D-ribose 1-diphosphate + 2 H(+) + quinolinate;
CC Xref=Rhea:RHEA:12733, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:29959, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC ChEBI:CHEBI:58017; EC=2.4.2.19;
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1.
CC -!- SUBUNIT: Hexamer formed by 3 homodimers. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR EMBL; U65510; AAC45128.1; -; Genomic_DNA.
DR PIR; T51326; T51326.
DR RefSeq; WP_011389186.1; NZ_CP077803.1.
DR AlphaFoldDB; P77938; -.
DR SMR; P77938; -.
DR OMA; DMIMLKD; -.
DR UniPathway; UPA00253; UER00331.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009435; P:NAD biosynthetic process; IMP:CACAO.
DR CDD; cd01572; QPRTase; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.90.1170.20; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004393; NadC.
DR InterPro; IPR027277; NadC/ModD.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR PANTHER; PTHR32179; PTHR32179; 1.
DR Pfam; PF01729; QRPTase_C; 1.
DR Pfam; PF02749; QRPTase_N; 1.
DR PIRSF; PIRSF006250; NadC_ModD; 1.
DR SUPFAM; SSF51690; SSF51690; 1.
DR TIGRFAMs; TIGR00078; nadC; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Pyridine nucleotide biosynthesis; Transferase.
FT CHAIN 1..296
FT /note="Probable nicotinate-nucleotide pyrophosphorylase
FT [carboxylating]"
FT /id="PRO_0000155948"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 140..142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 249..251
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 270..272
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 296 AA; 30536 MW; 96605A621C84DCAE CRC64;
MRPNHPVAAL SPFAIDEAVR RALAEDLGRA GDITSTATIP AATRAHARFV ARQPGILAGL
GCARSAFALL DDTVTFTTPL EDGAEIAAGQ TVAEVAGAAR TILAAERTAL NFLGHLSGIA
TRTRRFGDAI AHTRARLTCT RKTTPGLRGL EKYAVRCGGG SNHRFGLDDA VLIKDNHIAV
AGGVSAALSR ARAGVGHMVR IEIEVDTLEQ LAEVLAVGGA EVVLLDNMDA PTLTRAVDMV
AGRLVTEASG GVSLDTIAAL AESGVDYISV GALTHSVTTL DIGLDIVVAP PKAERA