ID I1CYV1_9PSEU Unreviewed; 425 AA.
AC I1CYV1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=hydroxyacid-oxoacid transhydrogenase {ECO:0000256|ARBA:ARBA00013182};
DE EC=1.1.99.24 {ECO:0000256|ARBA:ARBA00013182};
GN ORFNames=SacglDRAFT_00938 {ECO:0000313|EMBL:EIE97875.1};
OS Saccharomonospora glauca K62.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=928724 {ECO:0000313|EMBL:EIE97875.1, ECO:0000313|Proteomes:UP000005087};
RN [1] {ECO:0000313|EMBL:EIE97875.1, ECO:0000313|Proteomes:UP000005087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K62 {ECO:0000313|EMBL:EIE97875.1,
RC ECO:0000313|Proteomes:UP000005087};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Brambilla E., Klenk H.-P., Woyke T.J.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K62 {ECO:0000313|Proteomes:UP000005087};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA Klenk H.-P., Woyke T.;
RT "Noncontiguous Finished sequence of chromosome of Saccharomonospora glauca
RT K62.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001484; EIE97875.1; -; Genomic_DNA.
DR RefSeq; WP_005462130.1; NZ_CM001484.1.
DR AlphaFoldDB; I1CYV1; -.
DR STRING; 928724.SacglDRAFT_00938; -.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_0_7_11; -.
DR OrthoDB; 323926at2; -.
DR Proteomes; UP000005087; Chromosome.
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; IPR018211; ADH_Fe_CS.
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.
DR PROSITE; PS00913; ADH_IRON_1; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005087};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 17..413
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 425 AA; 45181 MW; 0BA70550BD5EAD20 CRC64;
MANYLHETVF TWGATPLKFG AGAVDEIGHD LARQGAERVL ILTDPGVAAT GVPQRVAEAA
RSGGLTVEVY DGVHVEPTDA SVLEAVEFAR QSTWDGFVGV GGGSAIDTAK AVNLLTTHPA
DLFDYVNKPI GAAKAPPGPL KPLVAVPTTA GTGSETTPVC IMDFLDLKVK SGISHPSLRP
SLAVVDPLLT LSMPPRVTAA SGMDVLCHAL ESYTARPFHS FPRHTPQTRV AYNGANPISD
TWTEKALHLL ARSFRRAVLN GGDLDARTDM MLAATFAGMG FGNAGVHIPH ACAYPIAGRV
REYRPADYPQ DEPLVPHGES VSLTAPAAFR FTFPTDPERH LHAARILDPS GPEHPDPRER
LPRALISLMR DIGIPNGLGG VGYTSSDIPA LVEGAMKQQR LLTVAPRAVS ETDLEGILTD
SLENW
//
