ID PNCB2_PSEAE Reviewed; 398 AA. AC Q9HW26; DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 144. DE RecName: Full=Nicotinate phosphoribosyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00570}; DE Short=NAPRTase 2 {ECO:0000255|HAMAP-Rule:MF_00570}; DE EC=6.3.4.21 {ECO:0000255|HAMAP-Rule:MF_00570}; GN Name=pncB2 {ECO:0000255|HAMAP-Rule:MF_00570}; GN OrderedLocusNames=PA4376; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; 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 / RC 1C / 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}. 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; AE004091; AAG07764.1; -; Genomic_DNA. DR PIR; F83099; F83099. DR RefSeq; NP_253066.1; NC_002516.2. DR RefSeq; WP_003102657.1; NZ_QZGE01000004.1. DR PDB; 1YIR; X-ray; 2.10 A; A/B/C/D=2-398. DR PDBsum; 1YIR; -. DR AlphaFoldDB; Q9HW26; -. DR SMR; Q9HW26; -. DR STRING; 208964.PA4376; -. DR PaxDb; 208964-PA4376; -. DR DNASU; 881378; -. DR GeneID; 881378; -. DR KEGG; pae:PA4376; -. DR PATRIC; fig|208964.12.peg.4583; -. DR PseudoCAP; PA4376; -. DR HOGENOM; CLU_030991_1_0_6; -. DR InParanoid; Q9HW26; -. DR OrthoDB; 9771406at2; -. DR PhylomeDB; Q9HW26; -. DR BioCyc; PAER208964:G1FZ6-4462-MONOMER; -. DR UniPathway; UPA00253; UER00457. DR EvolutionaryTrace; Q9HW26; -. 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:0034355; P:NAD salvage; IBA:GO_Central. DR CDD; cd01401; PncB_like; 1. DR Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 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 NCBIfam; TIGR01514; NAPRTase; 1. DR PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1. DR PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1. DR Pfam; PF04095; NAPRTase; 1. DR Pfam; PF17767; NAPRTase_N; 1. DR PIRSF; PIRSF000484; NAPRT; 1. DR SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1. DR SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Ligase; Phosphoprotein; Pyridine nucleotide biosynthesis; KW Reference proteome. FT CHAIN 1..398 FT /note="Nicotinate phosphoribosyltransferase 2" FT /id="PRO_0000205838" FT MOD_RES 224 FT /note="Phosphohistidine; by autocatalysis" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00570" FT STRAND 16..18 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 19..31 FT /evidence="ECO:0007829|PDB:1YIR" FT STRAND 36..43 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 50..52 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 53..65 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 70..77 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 84..92 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:1YIR" FT STRAND 100..105 FT /evidence="ECO:0007829|PDB:1YIR" FT STRAND 108..116 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 117..120 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 124..139 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 145..160 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 165..168 FT /evidence="ECO:0007829|PDB:1YIR" FT STRAND 172..175 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 184..197 FT /evidence="ECO:0007829|PDB:1YIR" FT STRAND 199..207 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 208..213 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 224..233 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 237..239 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 240..252 FT /evidence="ECO:0007829|PDB:1YIR" FT STRAND 258..261 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 266..272 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 275..280 FT /evidence="ECO:0007829|PDB:1YIR" FT STRAND 283..286 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 291..305 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 309..311 FT /evidence="ECO:0007829|PDB:1YIR" FT STRAND 312..316 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 322..332 FT /evidence="ECO:0007829|PDB:1YIR" FT TURN 333..335 FT /evidence="ECO:0007829|PDB:1YIR" FT STRAND 336..342 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 344..347 FT /evidence="ECO:0007829|PDB:1YIR" FT STRAND 358..365 FT /evidence="ECO:0007829|PDB:1YIR" FT HELIX 386..395 FT /evidence="ECO:0007829|PDB:1YIR" SQ SEQUENCE 398 AA; 45691 MW; 526899B1B705C37F CRC64; MAESAFSERI VQNLLDTDFY KLTMMQAVLH NYPNAEVEWE FRCRNQEDLR LYLPAIREQL EYLAGLAISD EQLAFLERIP FLAPDFIRFL GLFRFNPRYV QTGIENDEFF LRLKGPWLHV ILFEVPLLAM ISEVRNRARY PAATVEQARE RLQEKFDWLR REASAEELAG FKMADFGTRR RFSYRVHEAV VSGLKEDFPG CFVGTSNVHL ARKLDLKPLG TMAHEWLMAH QQLGPRLIDS QSAALDCWVR EYRGLLGIAL TDCITTDAFL RDFDLYFAKL FDGLRHDSGD PLLWAEKTIA HYLKLGIDPL TKTLVFSDGL DLPRALKIYR ALQGRINVSF GIGTHFTCDL PGVEPMNIVV KMSACNGHPV AKISDTPGKA QCRDPDFIHY LKHVFQVA //