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}; 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 / 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; 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
//
