(data stored in ACNUC7421 zone)

SWISSPROT: B4SJ96_STRM5

ID   B4SJ96_STRM5            Unreviewed;       393 AA.
AC   B4SJ96;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00570, ECO:0000256|RuleBase:RU003838, ECO:0000256|SAAS:SAAS01089170};
DE            Short=NAPRTase {ECO:0000256|HAMAP-Rule:MF_00570};
DE            EC=6.3.4.21 {ECO:0000256|HAMAP-Rule:MF_00570, ECO:0000256|RuleBase:RU003838, ECO:0000256|SAAS:SAAS01130077};
GN   Name=pncB {ECO:0000256|HAMAP-Rule:MF_00570};
GN   OrderedLocusNames=Smal_0559 {ECO:0000313|EMBL:ACF50264.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50264.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50264.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50264.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the synthesis of beta-nicotinate D-
CC       ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate
CC       at the expense of ATP. {ECO:0000256|HAMAP-Rule:MF_00570,
CC       ECO:0000256|RuleBase:RU003838, ECO:0000256|SAAS:SAAS00377693}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O +
CC         nicotinate = ADP + diphosphate + nicotinate beta-D-
CC         ribonucleotide + phosphate; Xref=Rhea:RHEA:36163,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:32544,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57502,
CC         ChEBI:CHEBI:58017, ChEBI:CHEBI:456216; EC=6.3.4.21;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00570,
CC         ECO:0000256|RuleBase:RU003838, ECO:0000256|SAAS:SAAS01130070};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_00570, ECO:0000256|RuleBase:RU003838,
CC       ECO:0000256|SAAS:SAAS01130068}.
CC   -!- PTM: Transiently phosphorylated on a His residue during the
CC       reaction cycle. Phosphorylation strongly increases the affinity
CC       for substrates and increases the rate of nicotinate D-
CC       ribonucleotide production. Dephosphorylation regenerates the low-
CC       affinity form of the enzyme, leading to product release.
CC       {ECO:0000256|HAMAP-Rule:MF_00570, ECO:0000256|RuleBase:RU003838}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00570, ECO:0000256|RuleBase:RU003838,
CC       ECO:0000256|SAAS:SAAS00884590}.
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DR   EMBL; CP001111; ACF50264.1; -; Genomic_DNA.
DR   RefSeq; WP_012510022.1; NC_011071.1.
DR   STRING; 391008.Smal_0559; -.
DR   EnsemblBacteria; ACF50264; ACF50264; Smal_0559.
DR   KEGG; smt:Smal_0559; -.
DR   eggNOG; ENOG4107RH7; Bacteria.
DR   eggNOG; COG1488; LUCA.
DR   HOGENOM; HOG000284928; -.
DR   KO; K00763; -.
DR   OMA; GTSNVHF; -.
DR   OrthoDB; 241792at2; -.
DR   BioCyc; SMAL391008:SMAL_RS02855-MONOMER; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019357; P:nicotinate nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; B4SJ96.
DR   SWISS-2DPAGE; B4SJ96.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Glycosyltransferase {ECO:0000313|EMBL:ACF50264.1};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00570,
KW   ECO:0000256|RuleBase:RU003838, ECO:0000256|SAAS:SAAS01130075,
KW   ECO:0000313|EMBL:ACF50264.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00570};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00570,
KW   ECO:0000256|RuleBase:RU003838, ECO:0000256|SAAS:SAAS01132898};
KW   Transferase {ECO:0000313|EMBL:ACF50264.1}.
FT   DOMAIN        8    129       NAPRTase_N. {ECO:0000259|Pfam:PF17767}.
FT   DOMAIN      164    390       NAPRTase. {ECO:0000259|Pfam:PF04095}.
FT   MOD_RES     217    217       Phosphohistidine; by autocatalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_00570}.
SQ   SEQUENCE   393 AA;  45081 MW;  3F1453E6F7C456A8 CRC64;
     MPIIQSLLDT DLYKFTMMQA VLHQHPGAQV QYRFKCRTPG IDLAHYIDQI DEEIDHLCSL
     RFSDAELDYM RGLRFVKPDF ADFLGLFHLD RKYIQLRASK TVPGEIELDI TGPWLHTILF
     EVPLLAIINE VWFRNTTTAD FAEGERRLQA KAALLRDTPG FEQCRIADYG SRRRYSRDWH
     ARLLPLLRDA LGPQLVGTSN VHFARLYGMT PHGTMAHEYL QAFQALGPRL RDSQVAALES
     WAREYRGDLG IALSDVVGLD AFLRDFDMYF CKLFDGVRHD SGDPFDWGDR MLAHFQQRRV
     DPRSKVLVFS DGLDIVKVMR LYDYFRGRCQ VAFGVGTHLT NDLGPTPLNI VIKMVRCNGQ
     PVAKLSDSPG KSMCDDPGYL TYLRQVFELP QPE
//

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