ID E3RF72_PYRTT Unreviewed; 494 AA.
AC E3RF72;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=hydroxyacid-oxoacid transhydrogenase {ECO:0000256|ARBA:ARBA00013182};
DE EC=1.1.99.24 {ECO:0000256|ARBA:ARBA00013182};
GN ORFNames=PTT_05756 {ECO:0000313|EMBL:EFQ95627.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ95627.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ95627.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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}.
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DR EMBL; GL532638; EFQ95627.1; -; Genomic_DNA.
DR RefSeq; XP_003296277.1; XM_003296229.1.
DR AlphaFoldDB; E3RF72; -.
DR STRING; 861557.E3RF72; -.
DR EnsemblFungi; EFQ95627; EFQ95627; PTT_05756.
DR KEGG; pte:PTT_05756; -.
DR eggNOG; KOG3857; Eukaryota.
DR HOGENOM; CLU_007207_0_7_1; -.
DR OrthoDB; 5479153at2759; -.
DR Proteomes; UP000001067; 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:UP000001067};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 73..464
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 494 AA; 53731 MW; D1552D7C880D851E CRC64;
MVISTAIRIA PSRAARALNL LRTVQYTHPP SCPCHSNPNY HQSPSTIQQA RRHLATPLDQ
FQQKEYAFEM AASSIRFGPG CTKEVGMDFK NMGSKRVMVV TDPNVRKLDA MKQVIEGLER
EGVTYEIFDK VRVEPKDHSI KEAIDFAKPW RPDAYLAVGG GSVIDTAKLM NLYTTFPEAE
FLDFVNAPLG KGLPIPSKLF PLIAVPTTAG TGSETTGTAI FDLVSKRAKT GIAHRNLKPT
LGIVDPLNTR TMPSAVHASS GLDVLCHSLE SWTAIPYYER TPRPTNPINR PAYQGANPIS
DIFSLKALKD TVKYLPRAVR DPEDHEAQSQ MLLAATLAGV GFGNAGVHLC HGMSYPISGQ
NPGYKHAGYD VDHTIIPHGV SVAVTAPAVF KFTGASNPER HLAAAEAFGV DISNVKAESA
GEVLSEALAE FLVKLGDQPR GLKALGFGKE HLDQLVEGTI PQARVLMLAP SLDMQNIDAE
REQLRGLFED AMEY
//
