BDH2_DANRE
ID BDH2_DANRE Reviewed; 245 AA.
AC Q561X9; B8JI04;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=3-hydroxybutyrate dehydrogenase type 2;
DE EC=1.1.1.-;
DE EC=1.1.1.30 {ECO:0000250|UniProtKB:Q9BUT1};
DE AltName: Full=R-beta-hydroxybutyrate dehydrogenase;
GN Name=bdh2; ORFNames=si:dkey-162b23.2, zgc:110323;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
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., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=20550936; DOI=10.1016/j.cell.2010.04.040;
RA Devireddy L.R., Hart D.O., Goetz D.H., Green M.R.;
RT "A mammalian siderophore synthesized by an enzyme with a bacterial homolog
RT involved in enterobactin production.";
RL Cell 141:1006-1017(2010).
CC -!- FUNCTION: Dehydrogenase that mediates the formation of 2,5-
CC dihydroxybenzoic acid (2,5-DHBA), a siderophore that shares structural
CC similarities with bacterial enterobactin and associates with lcn2 (By
CC similarity). It thereby plays a key role in iron assimilation and
CC homeostasis (PubMed:20550936). Also acts as a 3-hydroxybutyrate
CC dehydrogenase (By similarity). {ECO:0000250|UniProtKB:Q8JZV9,
CC ECO:0000250|UniProtKB:Q9BUT1, ECO:0000269|PubMed:20550936}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-3-hydroxybutanoate + NAD(+) = acetoacetate + H(+) + NADH;
CC Xref=Rhea:RHEA:20521, ChEBI:CHEBI:10983, ChEBI:CHEBI:13705,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.30;
CC Evidence={ECO:0000250|UniProtKB:Q9BUT1};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000250|UniProtKB:Q8JZV9}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9BUT1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BUT1}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos.
CC {ECO:0000269|PubMed:20550936}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes no
CC gross defects in embryos, with the exception of hypochromic blood due
CC to decreased hemoglobin levels. {ECO:0000269|PubMed:20550936}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAX13853.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CR388005; CAX13852.1; -; Genomic_DNA.
DR EMBL; CR388005; CAX13853.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC092874; AAH92874.1; -; mRNA.
DR RefSeq; NP_001017809.1; NM_001017809.1.
DR RefSeq; XP_005160124.1; XM_005160067.3.
DR RefSeq; XP_005160125.1; XM_005160068.3.
DR AlphaFoldDB; Q561X9; -.
DR SMR; Q561X9; -.
DR STRING; 7955.ENSDARP00000069085; -.
DR PaxDb; Q561X9; -.
DR Ensembl; ENSDART00000074597; ENSDARP00000069085; ENSDARG00000052696.
DR Ensembl; ENSDART00000132542; ENSDARP00000119021; ENSDARG00000052696.
DR Ensembl; ENSDART00000181064; ENSDARP00000146933; ENSDARG00000052696.
DR GeneID; 550507; -.
DR KEGG; dre:550507; -.
DR CTD; 56898; -.
DR ZFIN; ZDB-GENE-050417-343; bdh2.
DR eggNOG; KOG0725; Eukaryota.
DR GeneTree; ENSGT00940000156721; -.
DR HOGENOM; CLU_010194_1_0_1; -.
DR InParanoid; Q561X9; -.
DR OMA; VYLCCKA; -.
DR OrthoDB; 1226147at2759; -.
DR PhylomeDB; Q561X9; -.
DR TreeFam; TF328795; -.
DR BRENDA; 1.1.1.30; 928.
DR Reactome; R-DRE-77111; Synthesis of Ketone Bodies.
DR PRO; PR:Q561X9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000052696; Expressed in head kidney and 21 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003858; F:3-hydroxybutyrate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; ISS:UniProtKB.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0043249; P:erythrocyte maturation; IMP:ZFIN.
DR GO; GO:0042168; P:heme metabolic process; IMP:UniProtKB.
DR GO; GO:0042541; P:hemoglobin biosynthetic process; IMP:ZFIN.
DR GO; GO:0055072; P:iron ion homeostasis; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019290; P:siderophore biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Lipid metabolism; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..245
FT /note="3-hydroxybutyrate dehydrogenase type 2"
FT /id="PRO_0000398629"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 16..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9BUT1"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9BUT1"
FT BINDING 58
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9BUT1"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9BUT1"
FT BINDING 180..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9BUT1"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ 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
