ID A0A2N6NXV1_BEABA Unreviewed; 501 AA.
AC A0A2N6NXV1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=hydroxyacid-oxoacid transhydrogenase {ECO:0000256|ARBA:ARBA00013182};
DE EC=1.1.99.24 {ECO:0000256|ARBA:ARBA00013182};
GN Name=Adhfe1 {ECO:0000313|EMBL:PMB72092.1};
GN ORFNames=BM221_002192 {ECO:0000313|EMBL:PMB72092.1};
OS Beauveria bassiana (White muscardine disease fungus) (Tritirachium
OS shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=176275 {ECO:0000313|EMBL:PMB72092.1, ECO:0000313|Proteomes:UP000235728};
RN [1] {ECO:0000313|EMBL:PMB72092.1, ECO:0000313|Proteomes:UP000235728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEF-007 {ECO:0000313|EMBL:PMB72092.1,
RC ECO:0000313|Proteomes:UP000235728};
RX PubMed=27470140; DOI=10.1007/s00253-016-7734-y;
RA Kim S., Lee S.J., Nai Y.S., Yu J.S., Lee M.R., Yang Y.T., Kim J.S.;
RT "Characterization of T-DNA insertion mutants with decreased virulence in
RT the entomopathogenic fungus Beauveria bassiana JEF-007.";
RL Appl. Microbiol. Biotechnol. 100:8889-8900(2016).
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:PMB72092.1}.
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DR EMBL; MRVG01000002; PMB72092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N6NXV1; -.
DR OMA; MNLYTTF; -.
DR Proteomes; UP000235728; 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:UP000235728};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 80..473
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT REGION 33..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 501 AA; 53588 MW; 06447A5AD28463FF CRC64;
MVSPIRVVPN AAVRAGSLLR TIQYTHPPSC PCHSNPGYHQ SPPPTPLSRP SSSSRGTRRY
ATPTKTGETL KEYAFEMAAS SIRFGPGVTK EVGMDFANLG AKRVAVVTDR TVEKLDAMKQ
VVEGLTREGI PFEVFSDVRV EPKDSSVKEA IAWSRPYQPD AFLAVGGGSV MDTAKLMNLY
TCYPDADFLD FVNAPLGKGR PVDKPLKPLI AVPTTAGTGS ETTGTAIFDL VAKKAKTGVA
HRNLKPTLGI CDPLNTRTMP SAVKASSGLD VLCHSLESWT AIPYNERTPR PANPLLRPAY
QGANPISDVF SFHALRATVK YLPRAVRDPE DFEAQSEMLL ASTLAGVGFG NAGVHLCHGM
SYPISGQNPA GYRHAGYELP APLIPHGVSV AVSAPAVFRF TGASNPERHL AAAEVFGVDI
SNVKRESAGE VLAEALSKFL ADLGDQPSGL KDLGFGSEHI EALVEGTLPQ ARVLMLAPGL
AKELETERDQ LRTLFENALS H
//