ID E7F8T6_DANRE Unreviewed; 493 AA.
AC E7F8T6; A0A8M1RH67;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Nicotinamide phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00035036, ECO:0000256|PIRNR:PIRNR005943};
DE Short=NAmPRTase {ECO:0000256|PIRNR:PIRNR005943};
DE EC=2.4.2.12 {ECO:0000256|ARBA:ARBA00035024, ECO:0000256|PIRNR:PIRNR005943};
GN Name=nampt1 {ECO:0000313|ZFIN:ZDB-GENE-110420-1};
GN Synonyms=nampta {ECO:0000313|RefSeq:XP_002661386.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000069804};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000069804}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000069804};
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSDARP00000069804, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000069804,
RC ECO:0000313|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000313|RefSeq:XP_002661386.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_002661386.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-nicotinamide D-ribonucleotide + diphosphate = 5-phospho-
CC alpha-D-ribose 1-diphosphate + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16149, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.12;
CC Evidence={ECO:0000256|PIRNR:PIRNR005943};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinamide D-
CC ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and
CC nicotinamide: step 1/1. {ECO:0000256|ARBA:ARBA00035007,
CC ECO:0000256|PIRNR:PIRNR005943}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR005943}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR005943}.
CC Cytoplasm {ECO:0000256|PIRNR:PIRNR005943}. Secreted
CC {ECO:0000256|PIRNR:PIRNR005943}.
CC -!- SIMILARITY: Belongs to the NAPRTase family.
CC {ECO:0000256|ARBA:ARBA00010897, ECO:0000256|PIRNR:PIRNR005943}.
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DR EMBL; CU928083; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002661386.1; XM_002661340.5.
DR STRING; 7955.ENSDARP00000069804; -.
DR PaxDb; 7955-ENSDARP00000069804; -.
DR PeptideAtlas; E7F8T6; -.
DR Ensembl; ENSDART00000075320; ENSDARP00000069804; ENSDARG00000030598.
DR Ensembl; ENSDART00000075320.6; ENSDARP00000069804.4; ENSDARG00000030598.8.
DR GeneID; 100330160; -.
DR KEGG; dre:100330160; -.
DR AGR; ZFIN:ZDB-GENE-110420-1; -.
DR CTD; 100330160; -.
DR ZFIN; ZDB-GENE-110420-1; nampt1.
DR eggNOG; ENOG502QSGN; Eukaryota.
DR HOGENOM; CLU_012550_2_0_1; -.
DR OMA; TFGFAMK; -.
DR OrthoDB; 312306at2759; -.
DR PhylomeDB; E7F8T6; -.
DR TreeFam; TF333530; -.
DR Reactome; R-DRE-197264; Nicotinamide salvaging.
DR UniPathway; UPA00253; UER00890.
DR PRO; PR:E7F8T6; -.
DR Proteomes; UP000000437; Chromosome 4.
DR Bgee; ENSDARG00000030598; Expressed in pharyngeal gill and 19 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047280; F:nicotinamide phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0032922; P:circadian regulation of gene expression; IEA:UniProtKB-UniRule.
DR GO; GO:0030097; P:hemopoiesis; IMP:ZFIN.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR CDD; cd01569; PBEF_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041529; DUF5598.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR016471; Nicotinamide_PRibTrfase.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR PANTHER; PTHR43816; NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43816:SF3; NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE-RELATED; 1.
DR Pfam; PF18127; NAMPT_N; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR PIRSF; PIRSF005943; NMPRT; 1.
DR SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Biological rhythms {ECO:0000256|PIRNR:PIRNR005943};
KW Cytokine {ECO:0000256|PIRNR:PIRNR005943};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR005943};
KW Glycosyltransferase {ECO:0000256|PIRNR:PIRNR005943,
KW ECO:0000313|RefSeq:XP_002661386.1};
KW Nucleus {ECO:0000256|PIRNR:PIRNR005943};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|PIRNR:PIRNR005943};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Secreted {ECO:0000256|PIRNR:PIRNR005943};
KW Transferase {ECO:0000256|PIRNR:PIRNR005943}.
FT DOMAIN 11..117
FT /note="Nicotinamide phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18127"
FT DOMAIN 189..466
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT BINDING 197
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
FT BINDING 220
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
FT BINDING 248
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
FT BINDING 312..314
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
FT BINDING 312
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
FT BINDING 354..355
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
FT BINDING 385
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
FT BINDING 393
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
SQ SEQUENCE 493 AA; 55932 MW; AC7BD6E528C5726D CRC64;
MEKHREAADF NILLATDSYK VTHYKQYPPN TSKVYSYFEC REKKTDSTKP RKVKYDKTVF
YGLQYILHKY LKGQVITPEK IQEAKEVYRE HFQDDVFNEK GWNYILEKYN GHLPIEIKAV
PEGSVIPRGN VLFTVENTDP ECYWLTNWVE TCLVQIWYPI TVATNSREQK KILAKYLMET
SGSLEGLEYK LHDFGYRGVS SQETAGIGAS AHLVNFKGTD TVAGIGVIKK YYGTKDPVPG
FSVPAAEHST ITAWGKDHEK DAFEHIIKQF PSVPVSIVSD SYDIYNACEK IWGEDLRSLI
EMRSADAPLV VRPDSGNPLD TVLKVLEILG KKFPPEENSK GYKVLPPYIR VIQGDGVDIN
TLQEIVEGMK EHRWSIENIA FGSGGALLQK LTRDLLNCSF KCSYVVTNGL GVNVFKDPVA
DPNKRSKKGR LSLHRTPSGD FVTLEEGKGD LEEYGEDLLH TVFRNGKIVK TYTFDEVRDN
AKLKESEVQD LLL
//
