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Database: UniProt
Entry: A0A0N0MWD2_9ACTN
LinkDB: A0A0N0MWD2_9ACTN
Original site: A0A0N0MWD2_9ACTN 
ID   A0A0N0MWD2_9ACTN        Unreviewed;       440 AA.
AC   A0A0N0MWD2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=hydroxyacid-oxoacid transhydrogenase {ECO:0000256|ARBA:ARBA00013182};
DE            EC=1.1.99.24 {ECO:0000256|ARBA:ARBA00013182};
GN   ORFNames=OK074_3275 {ECO:0000313|EMBL:KPI09469.1};
OS   Actinobacteria bacterium OK074.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI09469.1, ECO:0000313|Proteomes:UP000037991};
RN   [1] {ECO:0000313|EMBL:KPI09469.1, ECO:0000313|Proteomes:UP000037991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK074 {ECO:0000313|EMBL:KPI09469.1,
RC   ECO:0000313|Proteomes:UP000037991};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT   and OV320.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-3-hydroxybutanoate + 2-oxoglutarate = (R)-2-
CC         hydroxyglutarate + acetoacetate; Xref=Rhea:RHEA:23048,
CC         ChEBI:CHEBI:11047, ChEBI:CHEBI:13705, ChEBI:CHEBI:15801,
CC         ChEBI:CHEBI:16810; EC=1.1.99.24;
CC         Evidence={ECO:0000256|ARBA:ARBA00000813};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-hydroxybutanoate = (R)-2-hydroxyglutarate +
CC         succinate semialdehyde; Xref=Rhea:RHEA:24734, ChEBI:CHEBI:15801,
CC         ChEBI:CHEBI:16724, ChEBI:CHEBI:16810, ChEBI:CHEBI:57706;
CC         EC=1.1.99.24; Evidence={ECO:0000256|ARBA:ARBA00001110};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. Hydroxyacid-oxoacid transhydrogenase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010005}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPI09469.1}.
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DR   EMBL; LJCV01000242; KPI09469.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0MWD2; -.
DR   PATRIC; fig|1592327.3.peg.5396; -.
DR   Proteomes; UP000037991; Unassembled WGS sequence.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0047988; F:hydroxyacid-oxoacid transhydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd08190; HOT; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR018211; ADH_Fe_CS.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   InterPro; IPR042157; HOT.
DR   PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR11496:SF83; HYDROXYACID-OXOACID TRANSHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR   PROSITE; PS00913; ADH_IRON_1; 1.
PE   3: Inferred from homology;
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KPI09469.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          29..430
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   440 AA;  45710 MW;  F1C89EF20663DC82 CRC64;
     MIAGGNIVEI NLPLSVHEEI ITWNAPPMKF GVGATREIGY ELVRAGLRSV LLVADPHLSR
     TGAAGRLAKL IEQDGVAVEV FDRVRIEPTD TSCTEAAAEL AHLDVDGYVA FGGGSTIDTA
     KMLNLLGSYP GGAVRDYLNK PVGAGAAVPG PLKPLVAVPT TAGSGSECTA MVALGITGLG
     GLKTGISNRE LRPSLALVDP MNTLTAPAQV TASSGYDVLT HACESYTARP YDRRAPYASP
     ADRPLYIGAN PISDVWAEQA LKLVGRFLRR AVLNPHDVEA RIAMSQAASF AAMGFGNAGT
     HLPHACAYPV AGLVRDYLPP GYGAEHAMVP HGSAVVSTAA AAFAFTYPTA PERHLRAAEL
     LGANLDGITA ANGADVLPAT LLSIVADTQG PLGIGSFGYT RRDLAALVDG ALQQQRLLVC
     CPRQADAEDL HRILDASLAG
//
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