NADC_PSEAE
ID NADC_PSEAE Reviewed; 282 AA.
AC P30819;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Nicotinate-nucleotide pyrophosphorylase [carboxylating];
DE EC=2.4.2.19;
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating];
DE Short=QAPRTase;
GN Name=nadC; OrderedLocusNames=PA4524;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 252-282.
RC STRAIN=ATCC 29260 / PA103, and PAK;
RX PubMed=2430961; DOI=10.1016/s0021-9258(18)66774-2;
RA Johnson K., Parker M.L., Lory S.;
RT "Nucleotide sequence and transcriptional initiation site of two Pseudomonas
RT aeruginosa pilin genes.";
RL J. Biol. Chem. 261:15703-15708(1986).
RN [3]
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: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; AE004091; AAG07912.1; -; Genomic_DNA.
DR EMBL; M14849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M14850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; G83080; G83080.
DR RefSeq; NP_253214.1; NC_002516.2.
DR RefSeq; WP_003104915.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; P30819; -.
DR SMR; P30819; -.
DR STRING; 287.DR97_1703; -.
DR PaxDb; P30819; -.
DR PRIDE; P30819; -.
DR EnsemblBacteria; AAG07912; AAG07912; PA4524.
DR GeneID; 878422; -.
DR KEGG; pae:PA4524; -.
DR PATRIC; fig|208964.12.peg.4735; -.
DR PseudoCAP; PA4524; -.
DR HOGENOM; CLU_039622_0_3_6; -.
DR InParanoid; P30819; -.
DR OMA; DMIMLKD; -.
DR PhylomeDB; P30819; -.
DR BioCyc; PAER208964:G1FZ6-4613-MON; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IBA:GO_Central.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Glycosyltransferase; Pyridine nucleotide biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..282
FT /note="Nicotinate-nucleotide pyrophosphorylase
FT [carboxylating]"
FT /id="PRO_0000155947"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 136..138
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 243..245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 264..266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 259
FT /note="V -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 30552 MW; 77FB18D18331C217 CRC64;
MPNLTLADLQ GEIQANVRTA LAEDVGGGDL TAQLIDPQRE AEARVITREH ATIAGRAWVD
EVFRQVDPRV LVTWQVEDGQ RVEPNQMLFQ LKGPARALLT GERSALNFLQ LLSGTATRSQ
HYADLVAGTA VKLLDTRKTL PGLRLAQKYA VTCGGCHNHR IGLYDAFLIK ENHIAACGGI
DRAIAEARRI APGKPVEVEV ENLDELRQAL EAGADIVMLD ELSLDDMRTA VALTAGRAKL
EASGGINEGT LRNIAETGVD YISIGTLTKD VRAVDLSMRL TL
