ID   Q2GRZ8_CHAGB            Unreviewed;       514 AA.
AC   Q2GRZ8;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=hydroxyacid-oxoacid transhydrogenase {ECO:0000256|ARBA:ARBA00013182};
DE            EC=1.1.99.24 {ECO:0000256|ARBA:ARBA00013182};
GN   ORFNames=CHGG_09256 {ECO:0000313|EMBL:EAQ85242.1};
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ85242.1, ECO:0000313|Proteomes:UP000001056};
RN   [1] {ECO:0000313|Proteomes:UP000001056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC   {ECO:0000313|Proteomes:UP000001056};
RX   PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408034; EAQ85242.1; -; Genomic_DNA.
DR   RefSeq; XP_001227183.1; XM_001227182.1.
DR   AlphaFoldDB; Q2GRZ8; -.
DR   STRING; 306901.Q2GRZ8; -.
DR   GeneID; 4395399; -.
DR   VEuPathDB; FungiDB:CHGG_09256; -.
DR   eggNOG; KOG3857; Eukaryota.
DR   HOGENOM; CLU_007207_0_7_1; -.
DR   InParanoid; Q2GRZ8; -.
DR   OMA; NLMGAGC; -.
DR   OrthoDB; 5479153at2759; -.
DR   Proteomes; UP000001056; 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:UP000001056};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          94..486
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   514 AA;  55436 MW;  4E19A49F7D6C6936 CRC64;
     MGAATIRALP NRAARAVNLL RTVQFSHPPS CPCHSNPNHH HHAATAPSAL TTVSRFADRT
     SSLHGNITRG SSRGYATPRD PAQQKEYAFE MAASSIRFGP GVTREVGMDL ANMGAKRVAV
     VTDPTVDRLE AMRQVREALD AEGIEYRVYA KVVVEPKDYS VKEAIEWTKP YAPDAFLAVG
     GGSVMDTAKL MNLYSCYPDA DFLDFVNAPL GKGRPIDRKL KPLIAVPTTA GTGSETTGTA
     IFDLASRRAK TGVAHRNLKP TLGICDPLNT RTMPAAVKAA SGLDVLCHSL ESWTAIPFQE
     RTPRPANPIL RPAYQGANPI SDIFSLNALR QTVKYLPRSV RDPDDMEAQS EMLLASTLAG
     VGFGNAGVHL CHGMSYPISG QNPGYRHAGY EIDVPIIPHG VSVAVSAPAV FRFTGPSNPE
     RHLAAAEAFG VDVSSVKKES AGEVLAEALT KFLADLGDQP KGLKELGFGR EHIEELVEGT
     IPQARVLMLA PGLAKELEQE RDQLRRLFED ALEH
//