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Database: UniProt
Entry: F0XVG4_AURAN
LinkDB: F0XVG4_AURAN
Original site: F0XVG4_AURAN 
ID   F0XVG4_AURAN            Unreviewed;       553 AA.
AC   F0XVG4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
DE            EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
GN   ORFNames=AURANDRAFT_70017 {ECO:0000313|EMBL:EGB13143.1};
OS   Aureococcus anophagefferens (Harmful bloom alga).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC   Aureococcus.
OX   NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN   [1] {ECO:0000313|EMBL:EGB13143.1, ECO:0000313|Proteomes:UP000002729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX   PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA   Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA   Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA   Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA   Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA   Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA   Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT   "Niche of harmful alga Aureococcus anophagefferens revealed through
RT   ecogenomics.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
CC   -!- FUNCTION: Catalyzes the first step in the biosynthesis of NAD from
CC       nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-
CC       ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
CC       {ECO:0000256|RuleBase:RU365100}.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001240,
CC         ECO:0000256|RuleBase:RU365100};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from nicotinate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004952, ECO:0000256|RuleBase:RU365100}.
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:0000256|RuleBase:RU365100}.
CC   -!- SIMILARITY: Belongs to the NAPRTase family.
CC       {ECO:0000256|ARBA:ARBA00010897, ECO:0000256|RuleBase:RU365100}.
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DR   EMBL; GL833120; EGB13143.1; -; Genomic_DNA.
DR   RefSeq; XP_009032740.1; XM_009034492.1.
DR   AlphaFoldDB; F0XVG4; -.
DR   EnsemblProtists; EGB13143; EGB13143; AURANDRAFT_70017.
DR   GeneID; 20227714; -.
DR   KEGG; aaf:AURANDRAFT_70017; -.
DR   eggNOG; KOG2511; Eukaryota.
DR   InParanoid; F0XVG4; -.
DR   OMA; VYFPGSP; -.
DR   OrthoDB; 1333333at2759; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000002729; Unassembled WGS sequence.
DR   GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01570; NAPRTase_A; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR041619; NAPRTase_C.
DR   InterPro; IPR040727; NAPRTase_N.
DR   InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR   InterPro; IPR006405; Nic_PRibTrfase_pncB.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   NCBIfam; TIGR01513; NAPRTase_put; 1.
DR   PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF17956; NAPRTase_C; 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   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365100};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW   ECO:0000256|RuleBase:RU365100};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002729};
KW   Transferase {ECO:0000256|RuleBase:RU365100}.
FT   DOMAIN          24..150
FT                   /note="Nicotinate phosphoribosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
FT   DOMAIN          431..538
FT                   /note="Nicotinate phosphoribosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17956"
SQ   SEQUENCE   553 AA;  61044 MW;  78599D65F1ACFA29 CRC64;
     MACSPTTTAR KKARTPVNPL VGPLLTDFYQ ISMAYTYWKH GRHERPAVFE LYFRKNPFGG
     EFTIFGGLEE CLCYVENFKV TDDDVEYLRT LLPRAEDEFF EWIRSVDCSK VQIYAVREGT
     VVFPKCPLLR IHGPLAIAQL LETTLLNLVN FASLATTRVT TNAARMRLAA GPDKKLLEFG
     LRRAQGPDGG VSASRYAFQG GFDGTSNVLA GRLFPDLPVS GTHSHAFVQS YITGDELDGD
     GVLGGVNLAE AALTWRRRLG YEDAGSLHAG EFAAFVAYAL ANPTNFVALV DTYSTLETGL
     KNFVTVALAL KECGFAPKGV RIDSGDLAYL SRESRALFAG VVDAFRGTRH EATAACLEAV
     SIVASNDINE TVLLSLKEQG HAIDCYGIGT HLVTCQAQPA LGCVYKLVEI DGEPCIKLSN
     EIAKTTIPGA KSIYRLVSSA DVMLLDLLVP FSHAPPEVGE RILCRHPFDH QKRAYVTPSK
     VLDLHQLVFD GTRCDPDRSL IDIRDHCLEQ LRTVREDILR PLNPTPYKTS VTPALFTFFQ
     EIWQRNEPVR ELS
//
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