NADC_BACSU
ID NADC_BACSU Reviewed; 289 AA.
AC P39666;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable nicotinate-nucleotide pyrophosphorylase [carboxylating];
DE EC=2.4.2.19;
DE AltName: Full=General stress protein 70;
DE Short=GSP70;
DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating];
DE Short=QAPRTase;
GN Name=nadC; Synonyms=yrxB; OrderedLocusNames=BSU27860;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-270.
RC STRAIN=168;
RX PubMed=8444804; DOI=10.1128/jb.175.5.1423-1432.1993;
RA Sun D., Setlow P.L.;
RT "Cloning, nucleotide sequence, and regulation of the Bacillus subtilis nadB
RT gene and a nifS-like gene, both of which are essential for NAD
RT biosynthesis.";
RL J. Bacteriol. 175:1423-1432(1993).
RN [3]
RP PROTEIN SEQUENCE OF 1-22.
RC STRAIN=168 / IS58;
RX PubMed=9298659; DOI=10.1002/elps.1150180820;
RA Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT "First steps from a two-dimensional protein index towards a response-
RT regulation map for Bacillus subtilis.";
RL Electrophoresis 18:1451-1463(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. {ECO:0000250}.
CC -!- INDUCTION: By heat shock, salt stress, oxidative stress, glucose
CC limitation and oxygen limitation.
CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1, Leu-59 or Met-74 is the
CC initiator. {ECO:0000305}.
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DR EMBL; AL009126; CAB14746.1; -; Genomic_DNA.
DR EMBL; M98822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; G69663; G69663.
DR RefSeq; NP_390664.1; NC_000964.3.
DR RefSeq; WP_003229689.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P39666; -.
DR SMR; P39666; -.
DR STRING; 224308.BSU27860; -.
DR PaxDb; P39666; -.
DR PRIDE; P39666; -.
DR EnsemblBacteria; CAB14746; CAB14746; BSU_27860.
DR GeneID; 936245; -.
DR KEGG; bsu:BSU27860; -.
DR PATRIC; fig|224308.179.peg.3027; -.
DR eggNOG; COG0157; Bacteria.
DR InParanoid; P39666; -.
DR OMA; DMIMLKD; -.
DR PhylomeDB; P39666; -.
DR BioCyc; BSUB:BSU27860-MON; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000001570; 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 Direct protein sequencing; Glycosyltransferase;
KW Pyridine nucleotide biosynthesis; Reference proteome; Stress response;
KW Transferase.
FT CHAIN 1..289
FT /note="Probable nicotinate-nucleotide pyrophosphorylase
FT [carboxylating]"
FT /id="PRO_0000155941"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129..131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 237..239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 258..260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 289 AA; 31393 MW; BB97EBD36DCCD188 CRC64;
MNHLQLKKLL NHFFLEDIGT GDLTSQSIFG EQSCEAEIVA KSEGIFAGAA IIKEGFSLLD
ENVQSILHKK DGDMLHKGEV IAELHGPAAA LLSGERVVLN LIQRLSGIAT MTREAVRCLD
DEQIKICDTR KTTPGLRMLE KYAVRAGGGY NHRFGLYDGI MIKDNHIAAC GSILEACKKA
RQAAGHMVNI EVEIETEEQL REAIAAGADV IMFDNCPPDT VRHFAKLTPA NIKTEASGGI
TLESLPAFKG TGVNYISLGF LTHSVKSLDI SMDVTLSNES VEECCYVNS
