ID A0A267FV42_9PLAT Unreviewed; 479 AA.
AC A0A267FV42;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=hydroxyacid-oxoacid transhydrogenase {ECO:0000256|ARBA:ARBA00013182};
DE EC=1.1.99.24 {ECO:0000256|ARBA:ARBA00013182};
GN ORFNames=BOX15_Mlig014130g3 {ECO:0000313|EMBL:PAA85758.1},
GN BOX15_Mlig014130g8 {ECO:0000313|EMBL:PAA77685.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA77685.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA77685.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA77685.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA77685.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAA77685.1}.
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DR EMBL; NIVC01000730; PAA77685.1; -; Genomic_DNA.
DR EMBL; NIVC01000305; PAA85758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267FV42; -.
DR STRING; 282301.A0A267FV42; -.
DR Proteomes; UP000215902; 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:UP000215902};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 60..468
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 479 AA; 51396 MW; 8C33DA56A36BFE4F CRC64;
MTQQLRSRVL TAMREVLERG AGNACPAHSA CGHRHHGGVL RRCHQTVQET EYAFEMAVST
VRYGPGVTRE IGQDVVNLGA KRVLVFTDNN LAELPPFKKV ADSLASNSVP FDVYPDVRVE
PTDSSFKAAI KAAGAANYDA FIAVGGGSVI DTAKAANLYV TNPKADFLDY VNAPIGRGLP
VTHELKPLIA VPTTSGTGSE TTGVAVFDLE SMHAKTGIAN RALRPTLGLI DPDHTASMPN
RVSAYSGFDV VCHALESFTA LPFDQRTPRP IDPKLRPAYQ GSNPISDVWC RWALDASARY
FRRAVRNPSD SEARSAMHLA ACMAGVGFGN AGVHLCHGLS YPISGLGTSV SSGGYRSEGY
SDQHALIPHG LSVVITAPKV FEFTGAASPD RHLEAARLLG ADVTWKKRED AGKVLSDQVR
QLMHDLDVPD GLQALGFDAS HIDSLVEGVL PQQRLRSIAP CPQTRDDIAG IYQASMRAY
//
