PNCB_SALTY
ID PNCB_SALTY Reviewed; 400 AA.
AC P22253;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
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, ECO:0000269|PubMed:7503993, ECO:0000269|PubMed:9521740, ECO:0000269|PubMed:9521741};
GN Name=pncB {ECO:0000255|HAMAP-Rule:MF_00570}; OrderedLocusNames=STM1004;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP PATHWAY.
RX PubMed=1987148; DOI=10.1128/jb.173.2.536-540.1991;
RA Vinitsky A., Teng H., Grubmeyer C.T.;
RT "Cloning and nucleic acid sequence of the Salmonella typhimurium pncB gene
RT and structure of nicotinate phosphoribosyltransferase.";
RL J. Bacteriol. 173:536-540(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP PHOSPHORYLATION.
RX PubMed=7503993; DOI=10.1016/s0021-9258(19)74485-8;
RA Vinitsky A., Grubmeyer C.;
RT "A new paradigm for biochemical energy coupling. Salmonella typhimurium
RT nicotinate phosphoribosyltransferase.";
RL J. Biol. Chem. 268:26004-26010(1993).
RN [4]
RP PHOSPHORYLATION AT HIS-220, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8672422; DOI=10.1021/bi9517906;
RA Gross J., Rajavel M., Segura E., Grubmeyer C.;
RT "Energy coupling in Salmonella typhimurium nicotinic acid
RT phosphoribosyltransferase: identification of His-219 as site of
RT phosphorylation.";
RL Biochemistry 35:3917-3924(1996).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-220, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PHOSPHORYLATION AT HIS-220.
RX PubMed=9521740; DOI=10.1021/bi9720134;
RA Rajavel M., Lalo D., Gross J.W., Grubmeyer C.;
RT "Conversion of a cosubstrate to an inhibitor: phosphorylation mutants of
RT nicotinic acid phosphoribosyltransferase.";
RL Biochemistry 37:4181-4188(1998).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION, AND PATHWAY.
RX PubMed=9521741; DOI=10.1021/bi972014w;
RA Gross J.W., Rajavel M., Grubmeyer C.;
RT "Kinetic mechanism of nicotinic acid phosphoribosyltransferase:
RT implications for energy coupling.";
RL Biochemistry 37:4189-4199(1998).
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:1987148,
CC ECO:0000269|PubMed:7503993, ECO:0000269|PubMed:9521740,
CC ECO:0000269|PubMed:9521741}.
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:7503993,
CC ECO:0000269|PubMed:9521740, ECO:0000269|PubMed:9521741};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for nicotinate in the presence of ATP
CC {ECO:0000269|PubMed:7503993};
CC KM=0.3 mM for nicotinate in the absence of ATP
CC {ECO:0000269|PubMed:7503993, ECO:0000269|PubMed:9521740};
CC KM=22 uM for 5-phospho-alpha-D-ribose 1-diphosphate in the presence
CC of ATP {ECO:0000269|PubMed:7503993};
CC KM=4.5 mM for 5-phospho-alpha-D-ribose 1-diphosphate in the absence
CC of ATP {ECO:0000269|PubMed:7503993, ECO:0000269|PubMed:9521740};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00570, ECO:0000269|PubMed:1987148, ECO:0000269|PubMed:9521741}.
CC -!- PTM: Transiently phosphorylated on a His residue during the reaction
CC cycle (PubMed:9521740). Phosphorylation strongly increases the affinity
CC for substrates and increases the rate of nicotinate D-ribonucleotide
CC production. Dephosphorylation regenerates the low-affinity form of the
CC enzyme, leading to product release (PubMed:7503993, PubMed:9521740,
CC PubMed:9521741). {ECO:0000269|PubMed:7503993,
CC ECO:0000269|PubMed:9521740, ECO:0000269|PubMed:9521741}.
CC -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000255|HAMAP-
CC Rule:MF_00570}.
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DR EMBL; M55986; AAA27190.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19938.1; -; Genomic_DNA.
DR PIR; A39130; A39130.
DR RefSeq; NP_459979.1; NC_003197.2.
DR RefSeq; WP_000191399.1; NC_003197.2.
DR AlphaFoldDB; P22253; -.
DR SMR; P22253; -.
DR STRING; 99287.STM1004; -.
DR iPTMnet; P22253; -.
DR PaxDb; P22253; -.
DR EnsemblBacteria; AAL19938; AAL19938; STM1004.
DR GeneID; 1252522; -.
DR KEGG; stm:STM1004; -.
DR PATRIC; fig|99287.12.peg.1061; -.
DR HOGENOM; CLU_030991_1_0_6; -.
DR OMA; QAVFHRY; -.
DR PhylomeDB; P22253; -.
DR BioCyc; SENT99287:STM1004-MON; -.
DR BRENDA; 6.3.4.21; 5542.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR GO; GO:0034355; P:NAD salvage; IBA:GO_Central.
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; Luminescence; Phosphoprotein;
KW Photoprotein; Pyridine nucleotide biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1987148"
FT CHAIN 2..400
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_0000205846"
FT MOD_RES 220
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:8672422,
FT ECO:0000269|PubMed:9521740"
FT MUTAGEN 220
FT /note="H->E,N: Loss of ATP hydrolysis and
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:9521740"
SQ SEQUENCE 400 AA; 45661 MW; BA76FF5EF0D02F3A CRC64;
MTQFASPVLH SLLDTDAYKL HMQQAVFHHY YDVQVAAEFR CRGDDLLGIY ADAIREQVDA
MQHLRLLEDE FQWLSGLPFF KPDYLNWLRE FRYNPAQVCV TNDNGKLNIR LTGPWREVIM
WEVPLLAVIS ELVHHYRSPN AGVDQALDAL ESKLVDFTAL TANLDMSRFH LMDFGTRRRF
SREVQQAIVK RLQQESWFVG TSNYDLARRL ALTPMGTQAH EWFQAHQQIS PDLATSQRAA
LAAWLNEYPD QLGIALTDCI TMDAFLRDFG IEFASRYQGL RHDSGDPVAW GEKAIAHYEK
LGIDPLTKTL VFSDNLDLPK AVELYRHFAS RVQLSFGIGT RLTCDIPQVK PLNIVIKLVE
CNGKPVAKLS DSPGKTICHD KAFVRALRKA FDLPQVRKAS
