PNCB_ECOLI
ID PNCB_ECOLI Reviewed; 400 AA.
AC P18133;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
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};
GN OrderedLocusNames=b0931, JW0914;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=GEC70;
RX PubMed=2211655; DOI=10.1016/s0021-9258(18)38215-2;
RA Wubbolts M.G., Terpstra P., van Beilen J.B., Kingma J., Meesters H.A.R.,
RA Witholt B.;
RT "Variation of cofactor levels in Escherichia coli. Sequence analysis and
RT expression of the pncB gene encoding nicotinic acid
RT phosphoribosyltransferase.";
RL J. Biol. Chem. 265:17665-17672(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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, ECO:0000269|PubMed:2211655}.
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, ECO:0000269|PubMed:2211655};
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}.
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; J05568; AAA24400.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74017.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35683.1; -; Genomic_DNA.
DR PIR; JQ0756; JQ0756.
DR RefSeq; NP_415451.1; NC_000913.3.
DR RefSeq; WP_001307697.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P18133; -.
DR SMR; P18133; -.
DR BioGRID; 4261881; 11.
DR BioGRID; 850992; 1.
DR DIP; DIP-10521N; -.
DR IntAct; P18133; 19.
DR STRING; 511145.b0931; -.
DR jPOST; P18133; -.
DR PaxDb; P18133; -.
DR PRIDE; P18133; -.
DR EnsemblBacteria; AAC74017; AAC74017; b0931.
DR EnsemblBacteria; BAA35683; BAA35683; BAA35683.
DR GeneID; 946648; -.
DR KEGG; ecj:JW0914; -.
DR KEGG; eco:b0931; -.
DR PATRIC; fig|1411691.4.peg.1344; -.
DR EchoBASE; EB0735; -.
DR eggNOG; COG1488; Bacteria.
DR HOGENOM; CLU_030991_1_0_6; -.
DR InParanoid; P18133; -.
DR OMA; QAVFHRY; -.
DR PhylomeDB; P18133; -.
DR BioCyc; EcoCyc:NICOTINATEPRIBOSYLTRANS-MON; -.
DR BioCyc; MetaCyc:NICOTINATEPRIBOSYLTRANS-MON; -.
DR BRENDA; 6.3.4.21; 2026.
DR UniPathway; UPA00253; UER00457.
DR PRO; PR:P18133; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IDA:UniProtKB.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IDA:EcoCyc.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IDA:UniProtKB.
DR GO; GO:0034355; P:NAD salvage; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Direct protein sequencing; Ligase; Phosphoprotein;
KW Pyridine nucleotide biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2211655"
FT CHAIN 2..400
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_0000205828"
FT MOD_RES 220
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
SQ SEQUENCE 400 AA; 45897 MW; 1D5FFC61EBAAE1D9 CRC64;
MTQFASPVLH SLLDTDAYKL HMQQAVFHHY YDVHVAAEFR CRGDDLLGIY ADAIREQVQA
MQHLRLQDDE YQWLSALPFF KADYLNWLRE FRFNPEQVTV SNDNGKLDIR LSGPWREVIL
WEVPLLAVIS EMVHRYRSPQ ADVAQALDTL ESKLVDFSAL TAGLDMSRFH LMDFGTRRRF
SREVQETIVK RLQQESWFVG TSNYDLARRL SLTPMGTQAH EWFQAHQQIS PDLANSQRAA
LAAWLEEYPD QLGIALTDCI TMDAFLRDFG VEFASRYQGL RHDSGDPVEW GEKAIAHYEK
LGIDPQSKTL VFSDNLDLRK AVELYRHFSS RVQLSFGIGT RLTCDIPQVK PLNIVIKLVE
CNGKPVAKLS DSPGKTICHD KAFVRALRKA FDLPHIKKAS
