ID   PNCB1_MYCTO             Reviewed;         448 AA.
AC   P9WJI8; L0T9B3; Q10641;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Nicotinate phosphoribosyltransferase pncB1;
DE            Short=NAPRTase pncB1;
DE            EC=6.3.4.21;
GN   Name=pncB1; OrderedLocusNames=MT1372;
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).
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 (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   -!- 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK45636.1; -; Genomic_DNA.
DR   PIR; F70770; F70770.
DR   RefSeq; WP_003900321.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WJI8; -.
DR   SMR; P9WJI8; -.
DR   PRIDE; P9WJI8; -.
DR   EnsemblBacteria; AAK45636; AAK45636; MT1372.
DR   KEGG; mtc:MT1372; -.
DR   PATRIC; fig|83331.31.peg.1479; -.
DR   HOGENOM; CLU_025154_3_0_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; 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   3: Inferred from homology;
KW   Ligase; Phosphoprotein; Pyridine nucleotide biosynthesis; Transferase.
FT   CHAIN           1..448
FT                   /note="Nicotinate phosphoribosyltransferase pncB1"
FT                   /id="PRO_0000427822"
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;  47241 MW;  E3F926EE7EA35CE9 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
     ASGLRSLPAD GLKLAPGEPA IPTRTIPA