ID A0A1I3HWS7_9ACTN Unreviewed; 429 AA.
AC A0A1I3HWS7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=hydroxyacid-oxoacid transhydrogenase {ECO:0000256|ARBA:ARBA00013182};
DE EC=1.1.99.24 {ECO:0000256|ARBA:ARBA00013182};
GN ORFNames=SAMN05216561_10816 {ECO:0000313|EMBL:SFI40047.1};
OS Nocardioides psychrotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1005945 {ECO:0000313|EMBL:SFI40047.1, ECO:0000313|Proteomes:UP000198649};
RN [1] {ECO:0000313|EMBL:SFI40047.1, ECO:0000313|Proteomes:UP000198649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11156 {ECO:0000313|EMBL:SFI40047.1,
RC ECO:0000313|Proteomes:UP000198649};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOQG01000008; SFI40047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3HWS7; -.
DR STRING; 1005945.SAMN05216561_10816; -.
DR OrthoDB; 323926at2; -.
DR Proteomes; UP000198649; Unassembled WGS sequence.
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:UP000198649};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 22..418
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 429 AA; 44939 MW; 3173ECD333F8F682 CRC64;
MGPLGYLDRV TETVFTYASP ALKFGSGASA EIGHDLAGWG ARRVLLVTDP GVAATGHPAR
IAEQMAGFDL DVTTYDGARV EPTDESLDAA IAFARDAGPF DAIVAVGGGS AIDTAKAVNL
LTTNPGELMD YINAPVGKAR APINPLLPLV AVPTTTGTGS ESTTICVLDV LALKVKTGIS
HALLRPRLAV VDPSLTLTQP TMVTAASGMD ILCHALESYT ARWYADFDAK RPEQRVPYCG
ANPVADVWSE KALSMLAASF RAAVRDGSDT VAREQMALAA TFAGLGFGNA GVHIPHANAY
PIAGRVRTFR PEGYPDDEAI VPHGMAVSLT APEAFRFTFD AAPERHLHAA RLLEPDVPGA
GPDVLPGVLA RLMRDIGIPN GLGEVGYGEG DVGDLVAGSL QQQRLLATAP KPVTDEDLEA
VFLGSMEHW
//