(data stored in ACNUC7421 zone)

SWISSPROT: Q5LWQ2_RUEPO

ID   Q5LWQ2_RUEPO            Unreviewed;       447 AA.
AC   Q5LWQ2;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 106.
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   ECO:0000313|EMBL:AAV93426.1};
GN   OrderedLocusNames=SPO0095 {ECO:0000313|EMBL:AAV93426.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93426.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93426.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93426.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93426.1; -; Genomic_DNA.
DR   STRING; 246200.SPO0095; -.
DR   EnsemblBacteria; AAV93426; AAV93426; SPO0095.
DR   KEGG; sil:SPO0095; -.
DR   eggNOG; ENOG4107RH7; Bacteria.
DR   eggNOG; COG1488; LUCA.
DR   HOGENOM; HOG000284929; -.
DR   KO; K00763; -.
DR   OMA; GTSNVHF; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000001023; 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   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; Q5LWQ2.
DR   SWISS-2DPAGE; Q5LWQ2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Glycosyltransferase {ECO:0000313|EMBL:AAV93426.1};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00570,
KW   ECO:0000256|RuleBase:RU003838, ECO:0000256|SAAS:SAAS01130075,
KW   ECO:0000313|EMBL:AAV93426.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   Transferase {ECO:0000313|EMBL:AAV93426.1}.
FT   DOMAIN       41    163       NAPRTase_N. {ECO:0000259|Pfam:PF17767}.
FT   DOMAIN      205    438       NAPRTase. {ECO:0000259|Pfam:PF04095}.
FT   MOD_RES     257    257       Phosphohistidine; by autocatalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_00570}.
SQ   SEQUENCE   447 AA;  51365 MW;  6CA6CD7A9543D78B CRC64;
     MAVRLAYPWV IHSERGPSVD IATRVYNHKW KIDPIVRSLI DTDFYKLLMC QSVFRNKPDT
     QVTFSLINRT MRIPLARIID EGELREQLDH IRSLRLSRGE STWLRGNTFY GKRQMFRPDF
     MEWFEGLQLP PYHLERRDDQ YELTFEGNWP EVMLWEIPAL AVLMELRSRA VLHDMRRFEL
     QVLYARAMTR VWEKIERLRG IDGLTIADFG TRRRHSFLWQ DWCVQAMIEG LGAKFTGTSN
     CLIAMRREVE AIGTNAHELP MVYSALAETD TELARAPYDV LSDWHEEHDG NLRIILPDTY
     GTKGFLDRAP DWLAGWTGIR IDSGDPAEGA ETAISWWKDR GENPTDKRII FSDGLDVDKI
     AELHARFSGR AKISFGWGTL LTNDFRGLVP DDGLAPFSLV CKAVSANGHP TVKLSDNPEK
     AMGPADEVAR YKRVFGVGRQ TSYAVEV
//

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