3HIDH_CAEEL
ID 3HIDH_CAEEL Reviewed; 299 AA.
AC Q9XTI0;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial;
DE Short=HIBADH;
DE EC=1.1.1.31;
GN ORFNames=B0250.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC dehydrogenase subfamily. {ECO:0000305}.
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DR EMBL; Z81453; CAB03798.1; -; Genomic_DNA.
DR EMBL; AL031630; CAB03798.1; JOINED; Genomic_DNA.
DR PIR; T18682; T18682.
DR RefSeq; NP_507943.1; NM_075542.6.
DR AlphaFoldDB; Q9XTI0; -.
DR SMR; Q9XTI0; -.
DR BioGRID; 45301; 11.
DR STRING; 6239.B0250.5; -.
DR iPTMnet; Q9XTI0; -.
DR EPD; Q9XTI0; -.
DR PaxDb; Q9XTI0; -.
DR PeptideAtlas; Q9XTI0; -.
DR EnsemblMetazoa; B0250.5.1; B0250.5.1; WBGene00007122.
DR GeneID; 180344; -.
DR UCSC; B0250.5; c. elegans.
DR CTD; 180344; -.
DR WormBase; B0250.5; CE18481; WBGene00007122; -.
DR eggNOG; KOG0409; Eukaryota.
DR GeneTree; ENSGT00940000173744; -.
DR HOGENOM; CLU_035117_6_0_1; -.
DR InParanoid; Q9XTI0; -.
DR OMA; WSSEVNN; -.
DR OrthoDB; 812358at2759; -.
DR PhylomeDB; Q9XTI0; -.
DR Reactome; R-CEL-70895; Branched-chain amino acid catabolism.
DR UniPathway; UPA00362; -.
DR PRO; PR:Q9XTI0; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00007122; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0008442; F:3-hydroxyisobutyrate dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR011548; HIBADH.
DR InterPro; IPR015815; HIBADH-related.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029154; NADP-bd.
DR Pfam; PF14833; NAD_binding_11; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000103; HIBADH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01692; HIBADH; 1.
DR PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE 3: Inferred from homology;
KW Branched-chain amino acid catabolism; Mitochondrion; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..299
FT /note="Probable 3-hydroxyisobutyrate dehydrogenase,
FT mitochondrial"
FT /id="PRO_0000173055"
FT ACT_SITE 172
FT /evidence="ECO:0000250"
FT BINDING 2..30
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 299 AA; 31217 MW; F30B423A597CABF0 CRC64;
MSLTGFIGLG NMGGHMARNL IKNGKKLIVY DVNKAVVQEF KAEGCEVAAH PADIAAASKE
IITVLPSSPH VKAVYQGEAG IFKTIQPGTL CMDSSTIDQI VSLEVAQAAA LLKAEYIDAP
ISGGVTGAQQ ATLTFMVGAG NDATFKRAEA VLSLMGKNIV NLGAVGNGTA AKICNNMLLG
IQMVAVAETM NLGISMGLDA KALAGIVNTS SGRCWSSDTY NPVPGVIENI PSCRGYAGGF
GTTLMAKDLS LAQNASTNTQ APTPMGSLAH QIYRILARDP QYQAKDFGVV YQFLKKQNS