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Database: UniProt
Entry: A0A1Y1YRH6_9PLEO
LinkDB: A0A1Y1YRH6_9PLEO
Original site: A0A1Y1YRH6_9PLEO 
ID   A0A1Y1YRH6_9PLEO        Unreviewed;       492 AA.
AC   A0A1Y1YRH6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=hydroxyacid-oxoacid transhydrogenase {ECO:0000256|ARBA:ARBA00013182};
DE            EC=1.1.99.24 {ECO:0000256|ARBA:ARBA00013182};
GN   ORFNames=BCR34DRAFT_606370 {ECO:0000313|EMBL:ORY00165.1};
OS   Clohesyomyces aquaticus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Lindgomycetaceae; Clohesyomyces.
OX   NCBI_TaxID=1231657 {ECO:0000313|EMBL:ORY00165.1, ECO:0000313|Proteomes:UP000193144};
RN   [1] {ECO:0000313|EMBL:ORY00165.1, ECO:0000313|Proteomes:UP000193144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115471 {ECO:0000313|EMBL:ORY00165.1,
RC   ECO:0000313|Proteomes:UP000193144};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORY00165.1}.
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DR   EMBL; MCFA01000187; ORY00165.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1YRH6; -.
DR   STRING; 1231657.A0A1Y1YRH6; -.
DR   OrthoDB; 5479153at2759; -.
DR   Proteomes; UP000193144; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; 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.
PE   3: Inferred from homology;
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193144};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          71..462
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   492 AA;  53271 MW;  5926857A67FFE515 CRC64;
     MAAIRIVPTR ATRALNLLRT VQFTHPPSCP CHSNPSHHHH HGNNMITAKR ALATPISTSQ
     QKEYAFEMAA SSIRFGPGCT KEVGMDFKNM GSKRVMVVTD PNVRKLEAMR QVTQALEREG
     VNFKVFDGVR VEPKDSSIKE AIEFARPWRP DAFLAVGGGS VIDTAKLMNL YTSCPEASFL
     DFVNAPLGLG LPITKKLFPL IAVPTTAGTG SETTGTAIFD LVEKRAKTGI AHRNLKPTLG
     IVDPLNTRTM PSAVHASSGL DVLCHSLESW TAIPFSERVP RPTNPINRPA YQGANPISDI
     FSLKALRDTV TYLPRAVKDP EDHEAQSAML LAATLAGVGF GNAGVHLCHG MSYPISGQNP
     GYQHPGYEVD HTIIPHGVSV AVTAPAVFKF TGASNPERHL AAAECFGVDI SQVKKESAGE
     VLGEALASFL VKLGDQPRGL KHLGFQNEHL DALVEGTIPQ ARVLMLAPSL EMQNVDVERE
     QLRGLFEEAM EY
//
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