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Database: UniProt
Entry: N1QCI9_PSEFD
LinkDB: N1QCI9_PSEFD
Original site: N1QCI9_PSEFD 
ID   N1QCI9_PSEFD            Unreviewed;       493 AA.
AC   N1QCI9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=hydroxyacid-oxoacid transhydrogenase {ECO:0000256|ARBA:ARBA00013182};
DE            EC=1.1.99.24 {ECO:0000256|ARBA:ARBA00013182};
GN   ORFNames=MYCFIDRAFT_55798 {ECO:0000313|EMBL:EME89377.1};
OS   Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS   fungus) (Mycosphaerella fijiensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=383855 {ECO:0000313|EMBL:EME89377.1, ECO:0000313|Proteomes:UP000016932};
RN   [1] {ECO:0000313|EMBL:EME89377.1, ECO:0000313|Proteomes:UP000016932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIRAD86 {ECO:0000313|EMBL:EME89377.1,
RC   ECO:0000313|Proteomes:UP000016932};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB446555; EME89377.1; -; Genomic_DNA.
DR   RefSeq; XP_007920184.1; XM_007921993.1.
DR   AlphaFoldDB; N1QCI9; -.
DR   STRING; 383855.N1QCI9; -.
DR   GeneID; 19340245; -.
DR   KEGG; pfj:MYCFIDRAFT_55798; -.
DR   eggNOG; KOG3857; Eukaryota.
DR   HOGENOM; CLU_007207_0_7_1; -.
DR   OrthoDB; 5479153at2759; -.
DR   Proteomes; UP000016932; 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:UP000016932};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          72..465
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   493 AA;  52830 MW;  559B7784FACF2907 CRC64;
     MPAIRVAPTR AQQAVGLLRA INSGTSTCPC HSNPGHHHHA QKNPTAGRVR SLATPVGSAH
     QQKEYAFEMA ASSIRFGPGC TKEVGMDFKN LHAKKVMVVT DSTVTKLDAM KQSIEGLERE
     GIAFHVFDKV KVEPKDYSIR EAIDFAKPYA PDAFLAVGGG SVIDTAKLMN LYTTCPDAEF
     LDFVNAPLGA GKPITSKLKP LIAVPTTAGT GSETTGTAIF DLVSKKAKTG IAHRNLKPTL
     GVCDPINTRT MPSAVHASSG LDVLCHSLES WTAIPYYERV PRPTNPINRP AYQGANPISD
     IFSLQALKDT VKYLPRAVKD PDDWEAQSKM LLAATLAGVG FGNAGVHLCH GMSYPISSQN
     PGYQHAGYEV QTPIIPHGVS VAVSAPAVFR FTGASNPERH LAAAEAFGVD VSNAKKDSAG
     EILSEALAEF LVKLGDQPRG LKALGFKNEH IDALVEGTMP QARVLMLAPN LEMQDTSAER
     EQLRGLFENA MEY
//
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