(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 130.
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}.
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   SMR; P30012; -.
DR   DrugBank; DB01796; Quinolinic Acid.
DR   PaxDb; P30012; -.
DR   PRIDE; P30012; -.
DR   EnsemblBacteria; AAL19109; AAL19109; STM0145.
DR   GeneID; 1251663; -.
DR   KEGG; stm:STM0145; -.
DR   PATRIC; fig|99287.12.peg.154; -.
DR   eggNOG; ENOG4105D18; Bacteria.
DR   eggNOG; COG0157; LUCA.
DR   HOGENOM; HOG000224022; -.
DR   KO; K00767; -.
DR   OMA; DMIMLKD; -.
DR   PhylomeDB; P30012; -.
DR   BioCyc; SENT99287:STM0145-MONOMER; -.
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;
DR   PRODOM; P30012.
DR   SWISS-2DPAGE; P30012.
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   REGION          152..154
FT                   /note="Substrate binding"
FT   REGION          259..261
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          280..282
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /note="Substrate"
FT                   /evidence="ECO:0000269|PubMed:9016724"
FT   BINDING         186
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="Blocked amino end (Pro)"
FT   HELIX           11..34
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   TURN            35..37
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   HELIX           41..43
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   HELIX           46..49
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   STRAND          59..64
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   HELIX           71..82
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   STRAND          85..91
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   STRAND          103..110
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   HELIX           111..140
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   TURN            141..144
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   STRAND          148..150
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   HELIX           160..170
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   STRAND          177..181
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   STRAND          183..185
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   HELIX           187..193
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   HELIX           196..206
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   STRAND          212..218
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   HELIX           219..227
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   STRAND          231..237
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   HELIX           240..248
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   STRAND          256..258
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   HELIX           264..272
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   STRAND          276..279
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   HELIX           282..285
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   STRAND          286..288
FT                   /evidence="ECO:0000244|PDB:1QAP"
FT   STRAND          292..295
FT                   /evidence="ECO:0000244|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
//

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