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Database: UniProt
Entry: G5DYA8_9PIPI
LinkDB: G5DYA8_9PIPI
Original site: G5DYA8_9PIPI 
ID   G5DYA8_9PIPI            Unreviewed;       191 AA.
AC   G5DYA8;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=3-hydroxyisobutyrate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00016933};
DE            EC=1.1.1.31 {ECO:0000256|ARBA:ARBA00012991};
DE   Flags: Fragment;
OS   Hymenochirus curtipes (western dwarf clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Pipinae; Hymenochirus.
OX   NCBI_TaxID=8362 {ECO:0000313|EMBL:AEQ17469.1};
RN   [1] {ECO:0000313|EMBL:AEQ17469.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver {ECO:0000313|EMBL:AEQ17469.1};
RA   Chain F.J.J., Evans B.J., Dushoff J.;
RT   "The odds of duplicate gene persistence after polyploidization.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-
CC         oxopropanoate + H(+) + NADH; Xref=Rhea:RHEA:17681, ChEBI:CHEBI:11805,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57700,
CC         ChEBI:CHEBI:57945; EC=1.1.1.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00000062};
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC       {ECO:0000256|ARBA:ARBA00005109}.
CC   -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC       dehydrogenase subfamily. {ECO:0000256|ARBA:ARBA00006013}.
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DR   EMBL; JP286122; AEQ17469.1; -; mRNA.
DR   AlphaFoldDB; G5DYA8; -.
DR   UniPathway; UPA00362; -.
DR   GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006574; P:valine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR029154; HIBADH-like_NADP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR22981:SF7; 3-HYDROXYISOBUTYRATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22981; 3-HYDROXYISOBUTYRATE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE   2: Evidence at transcript level;
KW   Branched-chain amino acid catabolism {ECO:0000256|ARBA:ARBA00022456};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          35..145
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          126..188
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEQ17469.1"
FT   NON_TER         191
FT                   /evidence="ECO:0000313|EMBL:AEQ17469.1"
SQ   SEQUENCE   191 AA;  20346 MW;  836EDE6C7EC17AE4 CRC64;
     MAALVRKSCS ALHRSVSRHA RLATVCRSMA SKTPVGFIGL GNMGNPMAKN LLKHGYPVVA
     FDVFPEACKD FQDSGAQITD SPADVAEKAD RIITMLPSSA NAIEVYTGSN GILKKVKKGS
     LLIDSSTIDP AVSKGFGTTL MAKDLGLAQN SATNTKSPTP LGSLSHQIYR LMCAKGYATK
     DFSSVFQFLR E
//
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