PNCB_YERPE
ID PNCB_YERPE Reviewed; 401 AA.
AC Q8ZG93; Q0WH02;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 144.
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=YPO1413, y2757, YP_1180;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM86309.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAS61423.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AL590842; CAL20065.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86309.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS61423.1; ALT_INIT; Genomic_DNA.
DR PIR; AG0172; AG0172.
DR RefSeq; WP_002228013.1; NZ_WUCM01000086.1.
DR RefSeq; YP_002346436.1; NC_003143.1.
DR PDB; 3OS4; X-ray; 1.60 A; A/B=1-401.
DR PDBsum; 3OS4; -.
DR AlphaFoldDB; Q8ZG93; -.
DR SMR; Q8ZG93; -.
DR STRING; 214092.YPO1413; -.
DR PaxDb; Q8ZG93; -.
DR PRIDE; Q8ZG93; -.
DR DNASU; 1147704; -.
DR EnsemblBacteria; AAM86309; AAM86309; y2757.
DR EnsemblBacteria; AAS61423; AAS61423; YP_1180.
DR GeneID; 66842128; -.
DR KEGG; ype:YPO1413; -.
DR KEGG; ypk:y2757; -.
DR KEGG; ypm:YP_1180; -.
DR PATRIC; fig|214092.21.peg.1740; -.
DR eggNOG; COG1488; Bacteria.
DR HOGENOM; CLU_030991_1_0_6; -.
DR OMA; QAVFHRY; -.
DR UniPathway; UPA00253; UER00457.
DR EvolutionaryTrace; Q8ZG93; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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: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..401
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_0000205855"
FT MOD_RES 221
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 17..29
FT /evidence="ECO:0007829|PDB:3OS4"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:3OS4"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3OS4"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:3OS4"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 122..137
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 143..160
FT /evidence="ECO:0007829|PDB:3OS4"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:3OS4"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 182..195
FT /evidence="ECO:0007829|PDB:3OS4"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:3OS4"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:3OS4"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 237..248
FT /evidence="ECO:0007829|PDB:3OS4"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:3OS4"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:3OS4"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:3OS4"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 319..329
FT /evidence="ECO:0007829|PDB:3OS4"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:3OS4"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:3OS4"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:3OS4"
FT HELIX 382..391
FT /evidence="ECO:0007829|PDB:3OS4"
SQ SEQUENCE 401 AA; 46022 MW; 88B37431DA649F2D CRC64;
MTQDASPILT SLLDTDAYKL HMQQAVFHHY RHITVAAEFR CRSDELLGVY ADEIRHQVTL
MGQLALTSDE FIYLSSLPFF QDDYLHWLRD FRFKPEQVSV AVHDGKLDIR IAGLWCEVIM
WEVPLLAVIS EIVHRRRSTQ VTTDQAVQQL RTKLEQFNAL SADIDITHFK LMDFGTRRRF
SREIQHTVVS TLKDEFPYLV GTSNYDLART LALAPVGTQA HEWFQAHQQI SPTLANSQRV
ALQVWLDEYP NQLGIALTDC ITMDAFLRDF DLAFANRYQG LRHDSGDPIE WGEKAIAHYE
KLGIDPMKKV LVFSDNLDLE KALFLYRHFY QRIKLVFGIG TRLTCDIPDV KPLNIVIKLV
ECNDKPVAKL SDSPGKTICQ DPAFVDQLRK AFALPLVKKA S
