ID   PNCB_VIBVY              Reviewed;         437 AA.
AC   Q7MK41;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00570};
DE            Short=NAPRTase {ECO:0000255|HAMAP-Rule:MF_00570};
DE            EC=6.3.4.21 {ECO:0000255|HAMAP-Rule:MF_00570};
GN   Name=pncB {ECO:0000255|HAMAP-Rule:MF_00570}; OrderedLocusNames=VV1969;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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:0000255|HAMAP-Rule:MF_00570}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00570};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00570}.
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:0000255|HAMAP-Rule:MF_00570}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00570}.
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DR   EMBL; BA000037; BAC94733.1; -; Genomic_DNA.
DR   RefSeq; WP_011150519.1; NC_005139.1.
DR   AlphaFoldDB; Q7MK41; -.
DR   SMR; Q7MK41; -.
DR   STRING; 672.VV93_v1c17290; -.
DR   EnsemblBacteria; BAC94733; BAC94733; BAC94733.
DR   KEGG; vvy:VV1969; -.
DR   PATRIC; fig|196600.6.peg.1997; -.
DR   eggNOG; COG1488; Bacteria.
DR   HOGENOM; CLU_030991_1_0_6; -.
DR   OMA; QAVFHRY; -.
DR   OrthoDB; 241792at2; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01401; PncB_like; 1.
DR   HAMAP; MF_00570; NAPRTase; 1.
DR   InterPro; IPR041525; N/Namide_PRibTrfase.
DR   InterPro; IPR040727; NAPRTase_N.
DR   InterPro; IPR006406; Nic_PRibTrfase.
DR   InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   PANTHER; PTHR11098; PTHR11098; 1.
DR   Pfam; PF04095; NAPRTase; 1.
DR   Pfam; PF17767; NAPRTase_N; 1.
DR   PIRSF; PIRSF000484; NAPRT; 1.
DR   SUPFAM; SSF51690; SSF51690; 1.
DR   TIGRFAMs; TIGR01514; NAPRTase; 1.
PE   3: Inferred from homology;
KW   Ligase; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..437
FT                   /note="Nicotinate phosphoribosyltransferase"
FT                   /id="PRO_0000205850"
FT   MOD_RES         231
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
SQ   SEQUENCE   437 AA;  49946 MW;  572E30CE2BA4FC9B CRC64;
     MCAPLFQPAI IQSVLDLDVY KINMMQAAYR FYPQTQVRYE LIVRSDDNLS DLVEEVREEI
     NRLAELRFDA AQLAYLAEKA PYLTAEFLSY LETFRFHPQQ QVSVGIFRTA QGDCQLRVTI
     NGIWHETILY ETLVMSIISE LRNRRYWAQI PQSQLHKVLE DKLDFLDSEL KRRNITNFRF
     SEMGTRRRFS FAAQKTMLDV LRARVPELLL GTSNYHLAQE FNLTPIGTVA HEWTMAHQAL
     VAVQHSQCVA LDKWLEAFNG SLGIALTDTI GIDAFLSDFD LEKATAYAGV RHDSGSPFVW
     GDKIIAHYES LGIDPSTKTL IFTDGLDFAR ALDICEYFAG RAQISFGIGT FLANDMGNWT
     NDKGIRYQPI SMVVKMAECN GSPVAKISDE PEKAMCEDIF FLMNLKQRFG LEVDLDKAIE
     TLKQMKRQQK KRIQSVA