NADC_ECOLI
ID NADC_ECOLI Reviewed; 297 AA.
AC P30011; Q2MCG5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 7.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating];
DE EC=2.4.2.19 {ECO:0000269|PubMed:8561507};
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000303|PubMed:8561507};
DE Short=QAPRTase;
GN Name=nadC; OrderedLocusNames=b0109, JW0105;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7959070; DOI=10.1016/0378-1119(94)90851-6;
RA Whitchurch C.B., Mattick J.S.;
RT "Escherichia coli contains a set of genes homologous to those involved in
RT protein secretion, DNA uptake and the assembly of type-4 fimbriae in other
RT bacteria.";
RL Gene 150:9-15(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=K12;
RX PubMed=8561507; DOI=10.1006/abbi.1996.0034;
RA Bhatia R.S., Calvo K.C.;
RT "The sequencing expression, purification, and steady-state kinetic analysis
RT of quinolinate phosphoribosyl transferase from Escherichia coli.";
RL Arch. Biochem. Biophys. 325:270-278(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116.
RC STRAIN=K12;
RX PubMed=2691840; DOI=10.1111/j.1365-2958.1989.tb00259.x;
RA Lindquist S., Galleni M., Lindberg F., Normark S.;
RT "Signalling proteins in enterobacterial AmpC beta-lactamase regulation.";
RL Mol. Microbiol. 3:1091-1102(1989).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116.
RC STRAIN=K12;
RX PubMed=2607970; DOI=10.1111/j.1365-2958.1989.tb00262.x;
RA Honore N., Nicolas M.H., Cole S.T.;
RT "Regulation of enterobacterial cephalosporinase production: the role of a
RT membrane-bound sensory transducer.";
RL Mol. Microbiol. 3:1121-1130(1989).
RN [8]
RP IDENTIFICATION.
RX PubMed=8419294; DOI=10.1128/jb.175.2.479-486.1993;
RA Hughes K.T., Dessen A., Gray J.P., Grubmeyer C.;
RT "The Salmonella typhimurium nadC gene: sequence determination by use of
RT Mud-P22 and purification of quinolinate phosphoribosyltransferase.";
RL J. Bacteriol. 175:479-486(1993).
CC -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC {ECO:0000269|PubMed:8561507}.
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 Evidence={ECO:0000269|PubMed:8561507};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12735;
CC Evidence={ECO:0000269|PubMed:8561507};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.6 uM for 5-phospho-alpha-D-ribose (at pH 7.8)
CC {ECO:0000269|PubMed:8561507};
CC KM=6.4 uM for quinolinate (at pH 7.8) {ECO:0000269|PubMed:8561507};
CC Vmax=0.96 umol/min/mg enzyme (at pH 7.8)
CC {ECO:0000269|PubMed:8561507};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from quinolinate: step 1/1.
CC {ECO:0000305|PubMed:8561507}.
CC -!- SUBUNIT: Homodimer Hexamer formed by 3 homodimers (By similarity).
CC Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR EMBL; L28105; AAC36922.1; -; Genomic_DNA.
DR EMBL; L20833; AAB00467.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73220.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76041.1; -; Genomic_DNA.
DR EMBL; X15237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; E64733; E64733.
DR RefSeq; NP_414651.1; NC_000913.3.
DR RefSeq; WP_001135174.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P30011; -.
DR SMR; P30011; -.
DR BioGRID; 4263544; 20.
DR DIP; DIP-10293N; -.
DR IntAct; P30011; 4.
DR STRING; 511145.b0109; -.
DR jPOST; P30011; -.
DR PaxDb; P30011; -.
DR PRIDE; P30011; -.
DR EnsemblBacteria; AAC73220; AAC73220; b0109.
DR EnsemblBacteria; BAE76041; BAE76041; BAE76041.
DR GeneID; 66671603; -.
DR GeneID; 948869; -.
DR KEGG; ecj:JW0105; -.
DR KEGG; eco:b0109; -.
DR PATRIC; fig|1411691.4.peg.2173; -.
DR EchoBASE; EB1508; -.
DR eggNOG; COG0157; Bacteria.
DR HOGENOM; CLU_039622_0_3_6; -.
DR InParanoid; P30011; -.
DR OMA; DMIMLKD; -.
DR PhylomeDB; P30011; -.
DR BioCyc; EcoCyc:QUINOPRIBOTRANS-MON; -.
DR BioCyc; MetaCyc:QUINOPRIBOTRANS-MON; -.
DR BRENDA; 2.4.2.19; 2026.
DR SABIO-RK; P30011; -.
DR UniPathway; UPA00253; UER00331.
DR PRO; PR:P30011; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IDA:EcoCyc.
DR GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IMP:EcoCyc.
DR GO; GO:0009435; P:NAD biosynthetic process; IDA:EcoliWiki.
DR GO; GO:0034213; P:quinolinate catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Glycosyltransferase; Pyridine nucleotide biosynthesis; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..297
FT /note="Nicotinate-nucleotide pyrophosphorylase
FT [carboxylating]"
FT /id="PRO_0000155942"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 152..154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 259..261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280..282
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 119
FT /note="R -> P (in Ref. 2; AAB00467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 32762 MW; 0B5DA69D9B67EE39 CRC64;
MPPRRYNPDT RRDELLERIN LDIPGAVAQA LREDLGGTVD ANNDITAKLL PENSRSHATV
ITRENGVFCG KRWVEEVFIQ LAGDDVTIIW HVDDGDVINA NQSLFELEGP SRVLLTGERT
ALNFVQTLSG VASKVRHYVE LLEGTNTQLL DTRKTLPGLR SALKYAVLCG GGANHRLGLS
DAFLIKENHI IASGSVRQAV EKASWLHPDA PVEVEVENLE ELDEALKAGA DIIMLDNFET
EQMREAVKRT NGKALLEVSG NVTDKTLREF AETGVDFISV GALTKHVQAL DLSMRFR
