NADC_SALTY
ID NADC_SALTY Reviewed; 297 AA.
AC P30012;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
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=STM0145;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=LT2;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP SUBUNIT.
RX PubMed=9016724; DOI=10.1016/s0969-2126(97)00165-2;
RA Eads J.C., Ozturk D., Wexler T.B., Grubmeyer C., Sacchettini J.C.;
RT "A new function for a common fold: the crystal structure of quinolinic acid
RT phosphoribosyltransferase.";
RL Structure 5:47-58(1997).
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 (By similarity). Homodimer.
CC {ECO:0000250, ECO:0000269|PubMed:9016724}.
CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
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DR EMBL; L07292; AAA03225.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19109.1; -; Genomic_DNA.
DR RefSeq; NP_459150.1; NC_003197.2.
DR RefSeq; WP_001135135.1; NC_003197.2.
DR PDB; 1QAP; X-ray; 2.80 A; A/B=2-297.
DR PDBsum; 1QAP; -.
DR AlphaFoldDB; P30012; -.
DR SMR; P30012; -.
DR STRING; 99287.STM0145; -.
DR DrugBank; DB01796; Quinolinic Acid.
DR PaxDb; P30012; -.
DR EnsemblBacteria; AAL19109; AAL19109; STM0145.
DR GeneID; 1251663; -.
DR KEGG; stm:STM0145; -.
DR PATRIC; fig|99287.12.peg.154; -.
DR HOGENOM; CLU_039622_0_3_6; -.
DR OMA; DMIMLKD; -.
DR PhylomeDB; P30012; -.
DR BioCyc; SENT99287:STM0145-MON; -.
DR UniPathway; UPA00253; UER00331.
DR EvolutionaryTrace; P30012; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosyltransferase;
KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..297
FT /note="Nicotinate-nucleotide pyrophosphorylase
FT [carboxylating]"
FT /id="PRO_0000155949"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 152..154
FT /ligand="substrate"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9016724"
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 MOD_RES 2
FT /note="Blocked amino end (Pro)"
FT HELIX 11..34
FT /evidence="ECO:0007829|PDB:1QAP"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1QAP"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1QAP"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:1QAP"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:1QAP"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:1QAP"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:1QAP"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:1QAP"
FT HELIX 111..140
FT /evidence="ECO:0007829|PDB:1QAP"
FT TURN 141..144
FT /evidence="ECO:0007829|PDB:1QAP"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1QAP"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:1QAP"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1QAP"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:1QAP"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:1QAP"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:1QAP"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:1QAP"
FT HELIX 219..227
FT /evidence="ECO:0007829|PDB:1QAP"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:1QAP"
FT HELIX 240..248
FT /evidence="ECO:0007829|PDB:1QAP"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:1QAP"
FT HELIX 264..272
FT /evidence="ECO:0007829|PDB:1QAP"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:1QAP"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:1QAP"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:1QAP"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:1QAP"
SQ SEQUENCE 297 AA; 32560 MW; 67F226C4D7C478ED CRC64;
MPPRRYNPDD RRDALLERIN LDIPAAVAQA LREDLGGEVD AGNDITAQLL PADTQAHATV
ITREDGVFCG KRWVEEVFIQ LAGDDVRLTW HVDDGDAIHA NQTVFELNGP ARVLLTGERT
ALNFVQTLSG VASEVRRYVG LLAGTQTQLL DTRKTLPGLR TALKYAVLCG GGANHRLGLT
DAFLIKENHI IASGSVRQAV EKAFWLHPDV PVEVEVENLD ELDDALKAGA DIIMLDNFNT
DQMREAVKRV NGQARLEVSG NVTAETLREF AETGVDFISV GALTKHVRAL DLSMRFC
