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3-hydroxybutyrate dehydrogenase type 2 (EC 1.1.1.-) (EC 1.1.1.30) (R-beta-hydroxybutyrate dehydrogenase)

 BDH2_DANRE              Reviewed;         245 AA.
Q561X9; B8JI04;
05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 1.
12-SEP-2018, entry version 99.
RecName: Full=3-hydroxybutyrate dehydrogenase type 2;
EC=1.1.1.-;
EC=1.1.1.30;
AltName: Full=R-beta-hydroxybutyrate dehydrogenase;
Name=bdh2; ORFNames=si:dkey-162b23.2, zgc:110323;
Danio rerio (Zebrafish) (Brachydanio rerio).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
Cyprinidae; Danio.
NCBI_TaxID=7955;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tuebingen;
PubMed=23594743; DOI=10.1038/nature12111;
Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
Stemple D.L.;
"The zebrafish reference genome sequence and its relationship to the
human genome.";
Nature 496:498-503(2013).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Olfactory epithelium;
NIH - Zebrafish Gene Collection (ZGC) project;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION.
PubMed=20550936; DOI=10.1016/j.cell.2010.04.040;
Devireddy L.R., Hart D.O., Goetz D.H., Green M.R.;
"A mammalian siderophore synthesized by an enzyme with a bacterial
homolog involved in enterobactin production.";
Cell 141:1006-1017(2010).
-!- FUNCTION: Dehydrogenase that mediates the formation of 2,5-
dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares
structural similarities with bacterial enterobactin and associates
with lcn2 (By similarity). It thereby plays a key role in iron
homeostasis and transport. {ECO:0000250,
ECO:0000269|PubMed:20550936}.
-!- CATALYTIC ACTIVITY: (R)-3-hydroxybutanoate + NAD(+) = acetoacetate
+ NADH.
-!- PATHWAY: Siderophore biosynthesis.
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAX13853.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; CR388005; CAX13852.1; -; Genomic_DNA.
EMBL; CR388005; CAX13853.1; ALT_SEQ; Genomic_DNA.
EMBL; BC092874; AAH92874.1; -; mRNA.
RefSeq; NP_001017809.1; NM_001017809.1.
RefSeq; XP_005160124.1; XM_005160067.3.
RefSeq; XP_005160125.1; XM_005160068.3.
UniGene; Dr.84969; -.
ProteinModelPortal; Q561X9; -.
SMR; Q561X9; -.
STRING; 7955.ENSDARP00000069085; -.
PaxDb; Q561X9; -.
Ensembl; ENSDART00000074597; ENSDARP00000069085; ENSDARG00000052696.
Ensembl; ENSDART00000132542; ENSDARP00000119021; ENSDARG00000052696.
Ensembl; ENSDART00000181064; ENSDARP00000146933; ENSDARG00000052696.
GeneID; 550507; -.
KEGG; dre:550507; -.
CTD; 56898; -.
ZFIN; ZDB-GENE-050417-343; bdh2.
eggNOG; KOG0725; Eukaryota.
eggNOG; COG1028; LUCA.
GeneTree; ENSGT00920000148965; -.
HOVERGEN; HBG002145; -.
InParanoid; Q561X9; -.
KO; K00019; -.
OMA; FPQWGAY; -.
OrthoDB; EOG091G0GO6; -.
PhylomeDB; Q561X9; -.
TreeFam; TF328795; -.
Reactome; R-DRE-77111; Synthesis of Ketone Bodies.
PRO; PR:Q561X9; -.
Proteomes; UP000000437; Chromosome 1.
Bgee; ENSDARG00000052696; Expressed in 29 organ(s), highest expression level in head kidney.
ExpressionAtlas; Q561X9; baseline and differential.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003858; F:3-hydroxybutyrate dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; ISS:UniProtKB.
GO; GO:0043249; P:erythrocyte maturation; IMP:ZFIN.
GO; GO:0042168; P:heme metabolic process; IMP:UniProtKB.
GO; GO:0042541; P:hemoglobin biosynthetic process; IMP:ZFIN.
GO; GO:0055072; P:iron ion homeostasis; ISS:UniProtKB.
GO; GO:0019290; P:siderophore biosynthetic process; ISS:UniProtKB.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
PRINTS; PR00081; GDHRDH.
PRINTS; PR00080; SDRFAMILY.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
2: Evidence at transcript level;
Complete proteome; Cytoplasm; NAD; Oxidoreductase; Reference proteome.
CHAIN 1 245 3-hydroxybutyrate dehydrogenase type 2.
/FTId=PRO_0000398629.
NP_BIND 10 37 NAD. {ECO:0000250}.
NP_BIND 180 184 NAD. {ECO:0000250}.
ACT_SITE 147 147 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10001}.
BINDING 58 58 NAD. {ECO:0000250}.
BINDING 144 144 Substrate. {ECO:0000250}.
BINDING 151 151 NAD. {ECO:0000250}.
BINDING 188 188 Substrate. {ECO:0000250}.
BINDING 205 205 Substrate. {ECO:0000250}.
SEQUENCE 245 AA; 26502 MW; 9D1B235692555D23 CRC64;
MGRLDGKVIV LSAAAQGIGK ASAIAFAKEG AQVTATDING EKLKELDGIP GIKTKVVDVT
KKDQVDALAK DFDHVDVLFN IAGFVHHGSI LDCEESDWDF TMNVNVRSMY LMIKAFLPKM
LARKSGNIIN MASVASSIKG VVNRCVYSTS KAAVIGLTKS VAADFLEQGI RCNCICPGTV
DTPSLRERIQ ARPDPEQAFK DFMARQRTGR LCTAEEVAHL CVYLASDEST FVTGTEVIID
GGWRL


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