ID G3QD50_GORGO Unreviewed; 467 AA.
AC G3QD50;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Hydroxyacid-oxoacid transhydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00021046};
DE EC=1.1.99.24 {ECO:0000256|ARBA:ARBA00013182};
DE AltName: Full=Alcohol dehydrogenase iron-containing protein 1 {ECO:0000256|ARBA:ARBA00032098};
GN Name=ADHFE1 {ECO:0000313|Ensembl:ENSGGOP00000000156.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000000156.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000000156.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000000156.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000000156.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; CABD030058394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030058395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004047159.1; XM_004047111.2.
DR AlphaFoldDB; G3QD50; -.
DR STRING; 9593.ENSGGOP00000000156; -.
DR Ensembl; ENSGGOT00000000159.3; ENSGGOP00000000156.3; ENSGGOG00000000157.3.
DR GeneID; 101130649; -.
DR KEGG; ggo:101130649; -.
DR CTD; 137872; -.
DR eggNOG; KOG3857; Eukaryota.
DR GeneTree; ENSGT00390000003849; -.
DR HOGENOM; CLU_007207_0_7_1; -.
DR InParanoid; G3QD50; -.
DR OMA; NLMGAGC; -.
DR OrthoDB; 5479153at2759; -.
DR TreeFam; TF105710; -.
DR Proteomes; UP000001519; Chromosome 8.
DR Bgee; ENSGGOG00000000157; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0047988; F:hydroxyacid-oxoacid transhydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006539; P:glutamate catabolic process via 2-oxoglutarate; IEA:Ensembl.
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:UP000001519};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 53..456
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 467 AA; 50315 MW; 0197937B504EBA1C CRC64;
MATAARARVA YLLRQLQRAA CQCPTHSHTY SQAPGLSPSG KTTDYAFEMA VSNIRYGAGV
TKEVGMDLQN MGAKNVCLMT DKNLSKLPPV QVAMDSLVKN GIPFTVYDNV RVEPTDASFM
EAIEFAQKGA FDAYVAVGGG STMDTCKAAN LYASSPHSDF LDYVSAPIGK GKPVSVPLKP
LIAVPTTSGT GSETTGVAIF DYEHLKVKIG ITSRAIKPTL GLIDPLHTLH MPARVVANSG
FDVLCHALES YTTLPYHLRS PCPSNPITRP AYQGSNPISD IWAIHALRIV AKYLKRAVRN
PDDLEARSHM HLASAFAGIG FGNAGVHLCH GMSYPISGLV KTYKAKDYNV DHPLVPHGLS
VVLTSPAVFT FTAQMFPERH LETAEILGAD TRTARIQDAG LVLAETLRKF LFDLDVDDGL
AAVGYSKADI PALVKGTLPQ ERVTKLAPRP QSEEDLAALF EASMKLY
//
