PNCB1_PSEAE
ID PNCB1_PSEAE Reviewed; 399 AA.
AC Q9HUP4;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Nicotinate phosphoribosyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00570};
DE Short=NAPRTase 1 {ECO:0000255|HAMAP-Rule:MF_00570};
DE EC=6.3.4.21 {ECO:0000255|HAMAP-Rule:MF_00570};
GN Name=pncB1 {ECO:0000255|HAMAP-Rule:MF_00570}; OrderedLocusNames=PA4919;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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; AE004091; AAG08304.1; -; Genomic_DNA.
DR PIR; E83030; E83030.
DR RefSeq; NP_253606.1; NC_002516.2.
DR RefSeq; WP_003099996.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HUP4; -.
DR SMR; Q9HUP4; -.
DR STRING; 287.DR97_2270; -.
DR PaxDb; Q9HUP4; -.
DR PRIDE; Q9HUP4; -.
DR EnsemblBacteria; AAG08304; AAG08304; PA4919.
DR GeneID; 882212; -.
DR KEGG; pae:PA4919; -.
DR PATRIC; fig|208964.12.peg.5152; -.
DR PseudoCAP; PA4919; -.
DR HOGENOM; CLU_030991_1_0_6; -.
DR InParanoid; Q9HUP4; -.
DR OMA; VMGFEIF; -.
DR PhylomeDB; Q9HUP4; -.
DR BioCyc; PAER208964:G1FZ6-5033-MON; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000002438; 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 3: Inferred from homology;
KW Ligase; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW Reference proteome.
FT CHAIN 1..399
FT /note="Nicotinate phosphoribosyltransferase 1"
FT /id="PRO_0000205837"
FT MOD_RES 224
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
SQ SEQUENCE 399 AA; 46095 MW; 49B2266CF47346DE CRC64;
MAESVFAERI VQNLLDTDFY KLTMMQAVLH NYPNAEVEWE FRCRNAEDLR PYLAEIRYQI
ERLAEVEVTA DQLAFLERIP FMKPDFIRFL SLFRFNLRYV HTGIEDGQLA IRLRGPWLHV
ILFEVPLLAI VSEVRNRYRY REVVLEQVGE QLYRKLDWLS AQASSEELAE FQVADFGTRR
RFSYRTQEEV VHILKRDFPG RFVGTSNVHL AREYDLKPIG TMAHEWLMAH QQLGPRLVDS
QQAALDCWVR EYRGQLGIAL TDCITMDAFL DDFDLYFAKL FDGLRHDSGD PLAWAEKAIA
HYRRLGIDPL SKTLVFSDGL DMPKALQLFR ALRGKINVSF GIGTNLTCDI PGVEPMNIVL
KMTACNGHPV AKISDAPGKT QCRDENFVAY LRHVFNVPA
