ID A0A0H1AQ22_9GAMM Unreviewed; 295 AA.
AC A0A0H1AQ22;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 ORFNames=WQ56_08410 {ECO:0000313|EMBL:KLJ00792.1};
OS Luteimonas sp. FCS-9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Luteimonas.
OX NCBI_TaxID=1547516 {ECO:0000313|EMBL:KLJ00792.1, ECO:0000313|Proteomes:UP000035397};
RN [1] {ECO:0000313|EMBL:KLJ00792.1, ECO:0000313|Proteomes:UP000035397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCS-9 {ECO:0000313|EMBL:KLJ00792.1,
RC ECO:0000313|Proteomes:UP000035397};
RA Bala M., Kumar A., Kaur N., Mathan Kumar R., Kaur G., Singh N.K.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Luteimonas oceanisediminis
RT sp. nov., a novel gammaproteobacteria isolated from a marine sediment.";
RL Submitted (APR-2015) 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|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}.
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:KLJ00792.1}.
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DR EMBL; LASZ01000007; KLJ00792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H1AQ22; -.
DR STRING; 1547516.WQ56_08410; -.
DR PATRIC; fig|1547516.3.peg.1773; -.
DR OrthoDB; 9786703at2; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000035397; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Branched-chain amino acid catabolism {ECO:0000256|ARBA:ARBA00022456,
KW ECO:0000256|RuleBase:RU910714}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000035397}.
FT DOMAIN 3..162
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 165..292
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 295 AA; 29316 MW; 6DBEA2B03171AA06 CRC64;
MTRIAFIGLG NMGGPMAANL AKAGHAVRAF DLSADALAAA SSAGVTAAVD AADTLADAEV
VLSMLPASRH VEGLYLGDEG LMAKIPDGAL VIDCSTIAPA SAQKVAAAAQ ARGLQMIDAP
VSGGTAGAQA GTLTFIVGGS ADALARARPV LEAMGKNIFH MGDTGAGQVA KLCNNMALGV
IMAATGEAIA LGVAHGLDPK VLSQMMAVST SRSWATEVCN PWPGVLENAP AGRGYTGGFG
NDLMLKDLGL AAEAAMGAGA AVPLGELARN LYAMNSQAGN GALDFSSVVK LLQRG
//
