ID   PNCB2_MYCTO             Reviewed;         463 AA.
AC   P9WJI6; L0T470; O53770; Q7D9M0;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Nicotinate phosphoribosyltransferase pncB2;
DE            Short=NAPRTase pncB2;
DE            EC=6.3.4.21;
GN   Name=pncB2; OrderedLocusNames=MT0601;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
RN   [2]
RP   INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12953092; DOI=10.1084/jem.20030205;
RA   Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M.,
RA   Sherman D.R., Schoolnik G.K.;
RT   "Inhibition of respiration by nitric oxide induces a Mycobacterium
RT   tuberculosis dormancy program.";
RL   J. Exp. Med. 198:705-713(2003).
CC   -!- FUNCTION: Involved in the Preiss-Handler pathway, which is a recycling
CC       route that permits the salvage of free nicotinamide (NM) and nicotinic
CC       acid (Na) involved in the NAD biosynthesis. Catalyzes the synthesis of
CC       beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose
CC       1-phosphate at the expense of ATP. It is not able to use nicotinamide.
CC       PncB2 appears to be responsible for the increased salvage synthesis of
CC       NAD during infection of host tissues (By similarity). {ECO:0000250}.
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   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1.
CC   -!- INDUCTION: A member of the dormancy regulon. Induced in response to
CC       reduced oxygen tension (hypoxia) and low levels of nitric oxide (NO).
CC       {ECO:0000269|PubMed:12953092}.
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; AE000516; AAK44824.1; -; Genomic_DNA.
DR   PIR; D70933; D70933.
DR   RefSeq; WP_003403007.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJI6; -.
DR   SMR; P9WJI6; -.
DR   EnsemblBacteria; AAK44824; AAK44824; MT0601.
DR   KEGG; mtc:MT0601; -.
DR   PATRIC; fig|83331.31.peg.633; -.
DR   HOGENOM; CLU_025154_3_1_11; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR041525; N/Namide_PRibTrfase.
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   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; TIGR01513; NAPRTase_put; 1.
PE   2: Evidence at transcript level;
KW   Ligase; Phosphoprotein; Pyridine nucleotide biosynthesis; Transferase.
FT   CHAIN           1..463
FT                   /note="Nicotinate phosphoribosyltransferase pncB2"
FT                   /id="PRO_0000427823"
FT   MOD_RES         202
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000250|UniProtKB:P22253"
SQ   SEQUENCE   463 AA;  50509 MW;  9D0B8745F869533A CRC64;
     MAIRQHVGAL FTDLYEVTMA QAYWAERMSG TAVFEIFFRK LPPGRSYIMA AGLADVVEFL
     EAFRFDEQDL RYLRGLGQFS DEFLRWLAGV RFTGDVWAAP EGTVIFPNEP AVQLIAPIIE
     AQLVETFVLN QIHLQSVLAS KAARVVAAAR GRPVVDFGAR RAHGTDAACK VARTSYLAGA
     AGTSNLLAAR QYGIPTFGTM AHSFVQAFDS EVAAFEAFAR LYPATMLLVD TYDTLRGVDH
     VIELAKRLGN RFDVRAVRLD SGDLDELSKA TRARLDTAGL EQVEIFASSG LDENRIAALL
     AARCPIDGFG VGTQLVVAQD APALDMAYKL VAYDGSGRTK FSSGKVIYPG RKQVFRKLEH
     GVFCGDTLGE HGENLPGDPL LVPIMTNGRR IRQHAPTLDG ARDWARQQID ALPPELRSLE
     DTGYSYPVAV SDRIVGELAR LRHADTAEAH PGSNVVGAKA KRP