ID   PNCB1_MYCTU             Reviewed;         448 AA.
AC   P9WJI9; L0T9B3; Q10641;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Nicotinate phosphoribosyltransferase pncB1;
DE            Short=NAPRTase pncB1;
DE            EC=6.3.4.21;
GN   Name=pncB1; OrderedLocusNames=Rv1330c; ORFNames=MTCY130.15c;
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   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND SUBSTRATE
RP   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   [3]
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       PncB1 contributes to basal NAD level. {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   -!- 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: Cells lacking this gene show a reduced
CC       incorporation of nicotinamide. Double mutants lacking both pncB1 and
CC       pncB2 show 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; CCP44088.1; -; Genomic_DNA.
DR   PIR; F70770; F70770.
DR   RefSeq; NP_215846.2; NC_000962.3.
DR   RefSeq; WP_003911483.1; NZ_NVQJ01000031.1.
DR   AlphaFoldDB; P9WJI9; -.
DR   SMR; P9WJI9; -.
DR   STRING; 83332.Rv1330c; -.
DR   PaxDb; P9WJI9; -.
DR   DNASU; 886884; -.
DR   GeneID; 886884; -.
DR   KEGG; mtu:Rv1330c; -.
DR   TubercuList; Rv1330c; -.
DR   eggNOG; COG1488; Bacteria.
DR   OMA; VYFPGSP; -.
DR   PhylomeDB; P9WJI9; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; 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   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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   InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR   PANTHER; PTHR11098; PTHR11098; 1.
DR   Pfam; PF17767; NAPRTase_N; 1.
DR   Pfam; PF01729; QRPTase_C; 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..448
FT                   /note="Nicotinate phosphoribosyltransferase pncB1"
FT                   /id="PRO_0000103804"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        357..372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         212
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000250|UniProtKB:P22253"
SQ   SEQUENCE   448 AA;  47227 MW;  E3F926EAA5835CE9 CRC64;
     MGPPPAARRR EGEPDNQDPA GLLTDKYELT MLAAALRDGS ANRPTTFEVF ARRLPTGRRY
     GVVAGTGRLL EALPQFRFDA DACELLAQFL DPATVRYLRE FRFRGDIDGY AEGELYFPGS
     PVLSVRGSFA ECVLLETLVL SIFNHDTAIA SAAARMVSAA GGRPLIEMGS RRTHERAAVA
     AARAAYIAGF AASSNLAAQR RYGVPAHGTA AHAFTMLHAQ HGGPTELAER AAFRAQVEAL
     GPGTTLLVDT YDVTTGVANA VAAAGAELGA IRIDSGELGV LARQAREQLD RLGATRTRIV
     VSGDLDEFSI AALRGEPVDS YGVGTSLVTG SGAPTANMVY KLVEVDGVPV QKRSSYKESP
     GGRKEALRRS RATGTITEEL VHPAGRPPVI VEPHRVLTLP LVRAGQPVAD TSLAAARQLV
     ASGLRSLPGD GLKLAPGEPA IPTRTIPA