ID   PNCB2_MYCTU             Reviewed;         463 AA.
AC   P9WJI7; 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 35.
DE   RecName: Full=Nicotinate phosphoribosyltransferase pncB2;
DE            Short=NAPRTase pncB2;
DE            EC=6.3.4.21;
GN   Name=pncB2; OrderedLocusNames=Rv0573c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   INDUCTION BY NITRIC OXIDE (NO) AND BY HYPOXIA, AND DORMANCY REGULON.
RC   STRAIN=ATCC 25618 / H37Rv;
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).
RN   [3]
RP   INDUCTION BY CARBON MONOXIDE (CO).
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=18474359; DOI=10.1016/j.chom.2008.03.007;
RA   Shiloh M.U., Manzanillo P., Cox J.S.;
RT   "Mycobacterium tuberculosis senses host-derived carbon monoxide during
RT   macrophage infection.";
RL   Cell Host Microbe 3:323-330(2008).
RN   [4]
RP   INDUCTION BY CARBON MONOXIDE (CO), AND DORMANCY REGULON.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=18400743; DOI=10.1074/jbc.m802274200;
RA   Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S., Kramnik I.,
RA   Agarwal A., Steyn A.J.;
RT   "Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium
RT   tuberculosis dormancy regulon.";
RL   J. Biol. Chem. 283:18032-18039(2008).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, INDUCTION BY HYPOXIA,
RP   AND SUBSTRATE SPECIFICITY.
RX   PubMed=18490451; DOI=10.1074/jbc.m800694200;
RA   Boshoff H.I., Xu X., Tahlan K., Dowd C.S., Pethe K., Camacho L.R.,
RA   Park T.H., Yun C.S., Schnappinger D., Ehrt S., Williams K.J.,
RA   Barry C.E. III;
RT   "Biosynthesis and recycling of nicotinamide cofactors in mycobacterium
RT   tuberculosis. An essential role for NAD in nonreplicating bacilli.";
RL   J. Biol. Chem. 283:19329-19341(2008).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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. {ECO:0000269|PubMed:18490451}.
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:0000269|PubMed:18490451};
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), low levels of nitric oxide (NO) and
CC       carbon monoxide (CO). It is hoped that this regulon will give insight
CC       into the latent, or dormant phase of infection.
CC       {ECO:0000269|PubMed:12953092, ECO:0000269|PubMed:18400743,
CC       ECO:0000269|PubMed:18474359, ECO:0000269|PubMed:18490451}.
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   -!- DISRUPTION PHENOTYPE: Double mutants lacking both pncB1 and pncB2 show
CC       an absence of incorporation of nicotinamide.
CC       {ECO:0000269|PubMed:18490451}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP43311.1; -; Genomic_DNA.
DR   PIR; D70933; D70933.
DR   RefSeq; NP_215087.1; NC_000962.3.
DR   RefSeq; WP_003403007.1; NZ_NVQJ01000036.1.
DR   AlphaFoldDB; P9WJI7; -.
DR   SMR; P9WJI7; -.
DR   STRING; 83332.Rv0573c; -.
DR   PaxDb; P9WJI7; -.
DR   DNASU; 887716; -.
DR   GeneID; 887716; -.
DR   KEGG; mtu:Rv0573c; -.
DR   TubercuList; Rv0573c; -.
DR   eggNOG; COG1488; Bacteria.
DR   OMA; TDTFAIQ; -.
DR   PhylomeDB; P9WJI7; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0047280; F:nicotinamide phosphoribosyltransferase activity; IDA:MTBBASE.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IDA:MTBBASE.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR   GO; GO:0009435; P:NAD biosynthetic process; IMP:MTBBASE.
DR   GO; GO:0034355; P:NAD salvage; IMP:MTBBASE.
DR   GO; GO:0075136; P:response to host; IEP:MTBBASE.
DR   GO; GO:0001666; P:response to hypoxia; IEP:MTBBASE.
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   1: Evidence at protein level;
KW   Ligase; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..463
FT                   /note="Nicotinate phosphoribosyltransferase pncB2"
FT                   /id="PRO_0000392685"
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