ID   PNCB_BACSU              Reviewed;         490 AA.
AC   O32090;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Nicotinate phosphoribosyltransferase;
DE            Short=NAPRTase;
DE            EC=6.3.4.21 {ECO:0000250|UniProtKB:P22253};
GN   Name=pncB; Synonyms=yueK; OrderedLocusNames=BSU31750;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; 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).
CC   -!- FUNCTION: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide
CC       from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of
CC       ATP. {ECO:0000250|UniProtKB:P22253}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O +
CC         nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide +
CC         phosphate; Xref=Rhea:RHEA:36163, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32544, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017,
CC         ChEBI:CHEBI:456216; EC=6.3.4.21;
CC         Evidence={ECO:0000250|UniProtKB:P22253};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1.
CC       {ECO:0000250|UniProtKB:P22253}.
CC   -!- PTM: Transiently phosphorylated on a His residue during the reaction
CC       cycle. Phosphorylation strongly increases the affinity for substrates
CC       and increases the rate of nicotinate D-ribonucleotide production.
CC       Dephosphorylation regenerates the low-affinity form of the enzyme,
CC       leading to product release. {ECO:0000250|UniProtKB:P22253}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000305}.
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DR   EMBL; AL009126; CAB15163.1; -; Genomic_DNA.
DR   PIR; D70008; D70008.
DR   RefSeq; NP_391053.1; NC_000964.3.
DR   RefSeq; WP_003228788.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O32090; -.
DR   SMR; O32090; -.
DR   IntAct; O32090; 1.
DR   MINT; O32090; -.
DR   STRING; 224308.BSU31750; -.
DR   jPOST; O32090; -.
DR   PaxDb; 224308-BSU31750; -.
DR   EnsemblBacteria; CAB15163; CAB15163; BSU_31750.
DR   GeneID; 937186; -.
DR   KEGG; bsu:BSU31750; -.
DR   PATRIC; fig|224308.179.peg.3441; -.
DR   eggNOG; COG1488; Bacteria.
DR   InParanoid; O32090; -.
DR   OrthoDB; 9770610at2; -.
DR   PhylomeDB; O32090; -.
DR   BioCyc; BSUB:BSU31750-MONOMER; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0034355; P:NAD salvage; IBA:GO_Central.
DR   CDD; cd01570; NAPRTase_A; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR041525; N/Namide_PRibTrfase.
DR   InterPro; IPR041619; NAPRTase_C.
DR   InterPro; IPR040727; NAPRTase_N.
DR   InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR   InterPro; IPR006405; Nic_PRibTrfase_pncB.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   NCBIfam; TIGR01513; NAPRTase_put; 1.
DR   PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF04095; NAPRTase; 1.
DR   Pfam; PF17956; NAPRTase_C; 1.
DR   Pfam; PF17767; NAPRTase_N; 1.
DR   PIRSF; PIRSF000484; NAPRT; 1.
DR   SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR   SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Ligase; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..490
FT                   /note="Nicotinate phosphoribosyltransferase"
FT                   /id="PRO_0000360847"
FT   MOD_RES         206
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000250|UniProtKB:P22253"
SQ   SEQUENCE   490 AA;  56180 MW;  02EC55FF5B3EF83D CRC64;
     MLEYGFKDDS LSLHTDLYQI NMAETYWRDG IHEKKAIFEL FFRRLPFENG YAVFAGLEKA
     IEYLENFKFT DSDLSYLQDE LGYHEDFIEY LRGLSFTGSL YSMKEGELVF NNEPIMRVEA
     PLVEAQLIET ALLNIVNYQT LIATKAARIK GVIGDEVALE FGTRRAHEMD AAMWGARAAL
     IGGFSATSNV RAGKRFNIPV SGTHAHALVQ AYRDEYTAFK KYAETHKDCV FLVDTYDTLR
     SGMPNAIRVA KEFGDRINFI GIRLDSGDLA YLSKKARKML DEAGFTDAKV IASSDLDEHT
     IMNLKAQGAR IDVWGVGTKL ITAYDQPALG AVYKLVAIEE DGKMVDTIKI SSNPEKVTTP
     GRKKVYRIIN QSNHHSEGDY IALYDEQVND QKRLRMFHPV HTFISKFVTN FYAKDLHELI
     FEKGILCYQN PEISDIQQYV QDNLSLLWEE YKRISKPEEY PVDLSEDCWS NKMQRIHEVK
     SRIEEELEEE
//