BDH2_LITCT
ID BDH2_LITCT Reviewed; 245 AA.
AC C1C4R8; C1C3Y0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 45.
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 Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Helbing C.C., Veldhoen N., Leong J., Koop B.F.;
RT "Rana catesbeiana ESTs and full-length cDNAs.";
RL Submitted (APR-2009) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BT081559; ACO51690.1; -; mRNA.
DR EMBL; BT081847; ACO51978.1; -; mRNA.
DR AlphaFoldDB; C1C4R8; -.
DR SMR; C1C4R8; -.
DR PRIDE; C1C4R8; -.
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.
FT CHAIN 1..245
FT /note="3-hydroxybutyrate dehydrogenase type 2"
FT /id="PRO_0000398630"
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"
FT CONFLICT 236
FT /note="A -> V (in Ref. 1; ACO51690)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 26587 MW; D639E805C9033DC8 CRC64;
MGRLDGKVIV LSAGAQGIGK AAAIAFAKEG AKVIATDING EKLKELESYK GIETRVLDVT
KKDQIEKLSK EIDRIDVLFN VAGFVHHGSI LDCEEADWDF TMNVNVRSMY LMIKTFLPKM
LAQKSGNIIN MSSVASSIKG VVNRCVYSTS KAAVIGLTKS VAADFIEQGI RCNCICPGTV
DTPSLRERIE ARPDPEQALK DFLARQKTGR MCTAEEVAHL CVYLASDEAA YVTGNAHIID
GGWSL