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Database: UniProt
Entry: Q6NRB2_XENLA
LinkDB: Q6NRB2_XENLA
Original site: Q6NRB2_XENLA 
ID   Q6NRB2_XENLA            Unreviewed;       328 AA.
AC   Q6NRB2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=3-hydroxyisobutyrate dehydrogenase {ECO:0000256|RuleBase:RU910714};
DE            Short=HIBADH {ECO:0000256|RuleBase:RU910714};
DE            EC=1.1.1.31 {ECO:0000256|RuleBase:RU910714};
GN   Name=hibadh.S {ECO:0000313|RefSeq:NP_001084759.1,
GN   ECO:0000313|Xenbase:XB-GENE-950894};
GN   Synonyms=hibadh {ECO:0000313|RefSeq:NP_001084759.1,
GN   ECO:0000313|Xenbase:XB-GENE-950894}, MGC84587
GN   {ECO:0000313|EMBL:AAH70849.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH70849.1};
RN   [1] {ECO:0000313|RefSeq:NP_001084759.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH70849.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocytes {ECO:0000313|EMBL:AAH70849.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001084759.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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         ECO:0000256|RuleBase:RU910714};
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC       {ECO:0000256|ARBA:ARBA00005109, ECO:0000256|RuleBase:RU910714}.
CC   -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC       dehydrogenase subfamily. {ECO:0000256|ARBA:ARBA00006013}.
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DR   EMBL; BC070849; AAH70849.1; -; mRNA.
DR   RefSeq; NP_001084759.1; NM_001091290.1.
DR   DNASU; 431794; -.
DR   GeneID; 431794; -.
DR   KEGG; xla:431794; -.
DR   AGR; Xenbase:XB-GENE-950894; -.
DR   CTD; 431794; -.
DR   Xenbase; XB-GENE-950894; hibadh.S.
DR   OrthoDB; 203032at2759; -.
DR   UniPathway; UPA00362; -.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 431794; Expressed in stomach and 19 other cell types or tissues.
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; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR011548; HIBADH.
DR   InterPro; IPR029154; HIBADH-like_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01692; HIBADH; 1.
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   PIRSF; PIRSF000103; HIBADH; 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   ECO:0000256|RuleBase:RU910714};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU910714};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU910714};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT   DOMAIN          35..193
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          196..322
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   328 AA;  34489 MW;  17A5ABEBD93C52D5 CRC64;
     MAALVRKSCS GLHSSVSRHA RFAMVCRSMA SKTPVGFIGL GNMGNPMARN LLKHGYPVVA
     FDVFPEACKD FQDSGAQIVD SPADVAEKAD RIITMLPSSA NATEVYTGSN GILKKVKKGS
     LLIDSSTIDP AVSKELAKGV EKMGAVFMDA PVSGGVGAAR SGNLTFMVGG VEQEFDAAKE
     LLSCMGANVV YCGAVGTGQA AKICNNMLLA ISMIGTSETM NLGIRLGLDP KLLAKILNMS
     SGRCWSSDTY NPVPGVMEGV PSANNYQGGF GTTLMAKDLG LAQDSATNTK SPTPLGSLAH
     QIYRVMCAKG YAQKDFSSVF QFLREEEN
//
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