ID   BDH2_XENLA              Reviewed;         245 AA.
AC   Q3KPT7;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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,
CC       thereby playing a key role in iron assimilation and homeostasis (By
CC       similarity). Also acts as a 3-hydroxybutyrate dehydrogenase (By
CC       similarity). {ECO:0000250|UniProtKB:Q8JZV9,
CC       ECO:0000250|UniProtKB:Q9BUT1}.
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   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; BC106561; AAI06562.1; -; mRNA.
DR   RefSeq; NP_001089786.1; NM_001096317.1.
DR   AlphaFoldDB; Q3KPT7; -.
DR   SMR; Q3KPT7; -.
DR   BioGRID; 592632; 1.
DR   GeneID; 734851; -.
DR   KEGG; xla:734851; -.
DR   CTD; 734851; -.
DR   Xenbase; XB-GENE-985759; bdh2.L.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 734851; Expressed in kidney and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003858; F:3-hydroxybutyrate dehydrogenase activity; IEA:UniProtKB-EC.
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:0042168; P:heme metabolic process; ISS:UniProtKB.
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_0000398631"
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;  26765 MW;  0A9E85F5B282DB6B CRC64;
     MGRLDGKVIV LSAAAQGIGR AAAIAFAKEG AQVIATDVNE MKLKELEAYK GIQTRVLDVT
     KKDQIENLCK EIDRIDVLFN VAGFVHHGTI LDCTEADWDF TMNVNVRSMY FMIKTFLPKM
     LAQKSGNIIN MSSVASSIKG VVNRCVYSTS KAAVIGLTKS VASDFIDQGI RCNCICPGTV
     DTPSLRERIQ ARPDPEQALK DFLARQRTGR MATAEEVAHL CVYLASDESA YVTGNEHIID
     GGWSL