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Database: UniProt
Entry: Q8EGC2_SHEON
LinkDB: Q8EGC2_SHEON
Original site: Q8EGC2_SHEON 
ID   Q8EGC2_SHEON            Unreviewed;       300 AA.
AC   Q8EGC2;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 134.
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=ivdF {ECO:0000313|EMBL:AAN54737.1};
GN   OrderedLocusNames=SO_1682 {ECO:0000313|EMBL:AAN54737.1};
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN54737.1, ECO:0000313|Proteomes:UP000008186};
RN   [1] {ECO:0000313|EMBL:AAN54737.1, ECO:0000313|Proteomes:UP000008186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1 {ECO:0000313|EMBL:AAN54737.1,
RC   ECO:0000313|Proteomes:UP000008186};
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA   Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA   Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA   Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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|RuleBase:RU910714};
CC   -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC       {ECO:0000256|RuleBase:RU910714}.
CC   -!- SIMILARITY: Belongs to the HIBADH-related family.
CC       {ECO:0000256|ARBA:ARBA00009080, ECO:0000256|RuleBase:RU910714}.
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DR   EMBL; AE014299; AAN54737.1; -; Genomic_DNA.
DR   RefSeq; NP_717293.1; NC_004347.2.
DR   RefSeq; WP_011071832.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EGC2; -.
DR   STRING; 211586.SO_1682; -.
DR   PaxDb; 211586-SO_1682; -.
DR   KEGG; son:SO_1682; -.
DR   PATRIC; fig|211586.12.peg.1622; -.
DR   eggNOG; COG2084; Bacteria.
DR   HOGENOM; CLU_035117_6_0_6; -.
DR   OrthoDB; 9786703at2; -.
DR   PhylomeDB; Q8EGC2; -.
DR   BioCyc; SONE211586:G1GMP-1548-MONOMER; -.
DR   UniPathway; UPA00362; -.
DR   Proteomes; UP000008186; Chromosome.
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: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; 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   3: Inferred from homology;
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:UP000008186}.
FT   DOMAIN          3..165
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          168..292
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   300 AA;  30819 MW;  1C410E00F635327B CRC64;
     MSTVAFIGLG NMGGPMAANL LKAGMTVRVF DLVHTAMQTL AEQGALVSST ACGAAAGANV
     VITMLPAGKH VKNLYLGSGS EKGLLDVVAS DTLLIDCSTI DAQSAQLVAT QAAKNGLEFM
     DAPVSGGTSG AAAGTLTFIC GGSDTAFERA QPVLNAMGKN IFHAGGPGAG QIAKICNNML
     LSVLMVGTSE ALQMGIDHGL DPKVLSNIMK VSSGGNWTLE KYNPCPGVME NVPSSKGYQG
     GFMVDLMVKD LGLSFEAALL SNSSTPMGAL ARSLYVSHAR QGNGHRDFSS IFEQFAPLKK
//
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