PNCB_VIBCH
ID PNCB_VIBCH Reviewed; 435 AA.
AC Q9KN67;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
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}; OrderedLocusNames=VC_A0098;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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}.
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};
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}.
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DR EMBL; AE003853; AAF96012.1; -; Genomic_DNA.
DR PIR; H82501; H82501.
DR RefSeq; NP_232499.1; NC_002506.1.
DR RefSeq; WP_001069589.1; NZ_LT906615.1.
DR PDB; 4HL7; X-ray; 1.80 A; A/B=2-435.
DR PDBsum; 4HL7; -.
DR AlphaFoldDB; Q9KN67; -.
DR SMR; Q9KN67; -.
DR STRING; 243277.VC_A0098; -.
DR PRIDE; Q9KN67; -.
DR DNASU; 2612706; -.
DR EnsemblBacteria; AAF96012; AAF96012; VC_A0098.
DR GeneID; 57741560; -.
DR KEGG; vch:VC_A0098; -.
DR PATRIC; fig|243277.26.peg.2739; -.
DR eggNOG; COG1488; Bacteria.
DR HOGENOM; CLU_030991_1_0_6; -.
DR OMA; QAVFHRY; -.
DR BioCyc; VCHO:VCA0098-MON; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000000584; Chromosome 2.
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: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 3D-structure; Ligase; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW Reference proteome.
FT CHAIN 1..435
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_0000205847"
FT MOD_RES 230
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:4HL7"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:4HL7"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:4HL7"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 50..62
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:4HL7"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:4HL7"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 153..172
FT /evidence="ECO:0007829|PDB:4HL7"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 190..203
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:4HL7"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 214..220
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 230..239
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:4HL7"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 271..277
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:4HL7"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 296..309
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:4HL7"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 327..337
FT /evidence="ECO:0007829|PDB:4HL7"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:4HL7"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:4HL7"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 398..407
FT /evidence="ECO:0007829|PDB:4HL7"
FT HELIX 414..425
FT /evidence="ECO:0007829|PDB:4HL7"
SQ SEQUENCE 435 AA; 50078 MW; 2CEF5D950C6C11FE CRC64;
MNPRLFSPHI IRSLLDLDAY KINMMQAIHH FYPDVSVRYE LIVRSEEDAS GLLDAIRQEI
AHLGTLRFSD ADIHYLTQHA PHLKATFLQS LRYFHFVPQE QVEMGIVKQG GKQQLRISIR
GSWRDTILYE TLVMAIVSEV RSRQRWAEVP ADLPLKVLKT KLDQLKAEIE RRGINNFSLT
EMGTRRRFSS QVQRDVLACL KQEIPQWVLG TSNYHFAREF DLKPIGTIAH EWFMGHQALV
NERDSQQVAL ERWLTAFDGM LAIAPTDTLT IDAFLNDFNR HLANAYDGVR HDSGCPFRWG
DKMIAHYQQL GIDPTTKLFI FSDGLDFDQA LELCEYFAGR VKISFGIGTF LTNDLANWRN
AAGVEYRPLS IVIKLAECQG RPVAKISDQP EKAMCEDPIF LANLKRRFNI ELDVDALIQE
LRHQKRSPRH YISAA
