ID A0A177D230_ALTAL Unreviewed; 494 AA.
AC A0A177D230;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=hydroxyacid-oxoacid transhydrogenase {ECO:0000256|ARBA:ARBA00013182};
DE EC=1.1.99.24 {ECO:0000256|ARBA:ARBA00013182};
GN ORFNames=AA0117_g4212 {ECO:0000313|EMBL:RYN78642.1}, CC77DRAFT_598375
GN {ECO:0000313|EMBL:OAG13664.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG13664.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG13664.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG13664.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000291422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FERA 1177 {ECO:0000313|Proteomes:UP000291422};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL bioRxiv 0:0-0(2019).
RN [3] {ECO:0000313|EMBL:RYN78642.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FERA 1177 {ECO:0000313|EMBL:RYN78642.1};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL J. ISSAAS 0:0-0(2019).
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; KV441507; OAG13664.1; -; Genomic_DNA.
DR EMBL; PDXD01000007; RYN78642.1; -; Genomic_DNA.
DR RefSeq; XP_018379085.1; XM_018532411.1.
DR STRING; 5599.A0A177D230; -.
DR GeneID; 29118005; -.
DR KEGG; aalt:CC77DRAFT_598375; -.
DR VEuPathDB; FungiDB:CC77DRAFT_598375; -.
DR OMA; NLMGAGC; -.
DR OrthoDB; 5479153at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR Proteomes; UP000291422; 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:UP000077248};
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; 53619 MW; F00824927AB82353 CRC64;
MVISTAIRIA PSRAARALNL LRTVQYTHPP SCPCHSNPNY HQSPATVQQA RRHLATPLDQ
FQQKEYAFEM AASSIRFGPG CTKEVGMDFK NMGSKRVMVV TDPNVRKLDA MKQVIEGLER
EGVTYEIFDK VRVEPKDHSI KEAIDFAKPW KPDAYLAVGG GSVIDTAKLM NLYTTFPEAD
FLDFVNAPLG KGMPIPSKLF PLIAVPTTAG TGSETTGTAI FDLVSKRAKT GIAHRNLKPT
LGIVDPLNTR TMPSAVHASS GLDVLCHSLE SWTAIPYYER TPRPTNPINR PAYQGANPIS
DIFSLKALKD TVKYLPRAVK DPDDHEAQSQ MLLAATLAGV GFGNAGVHLC HGMSYPISGQ
NPGYKHAGYD VDHTIIPHGV SVAVTAPAVF KFTGASNPER HLAAAEAFGV DISNVKAESA
GEVLGEALAE FLIKLGDQPR GLKALGFGKE HLDQLVEGTI PQARVLMLAP SLEMQNVDAE
REQLRGLFED AMEY
//
