ID A4XS20_PSEMY Unreviewed; 294 AA.
AC A4XS20;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
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 OrderedLocusNames=Pmen_1371 {ECO:0000313|EMBL:ABP84136.1};
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739 {ECO:0000313|EMBL:ABP84136.1};
RN [1] {ECO:0000313|EMBL:ABP84136.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ymp {ECO:0000313|EMBL:ABP84136.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-2007) 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}.
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DR EMBL; CP000680; ABP84136.1; -; Genomic_DNA.
DR AlphaFoldDB; A4XS20; -.
DR STRING; 399739.Pmen_1371; -.
DR KEGG; pmy:Pmen_1371; -.
DR PATRIC; fig|399739.8.peg.1390; -.
DR eggNOG; COG2084; Bacteria.
DR HOGENOM; CLU_035117_6_0_6; -.
DR OrthoDB; 9786703at2; -.
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; 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}.
FT DOMAIN 3..162
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 165..289
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 294 AA; 30320 MW; E9E8F39247D90BB5 CRC64;
MTQIAFIGLG HMGLPMAHNL LKAGYPLKVF DLVRSAVDTL AGEGAVAAES AADASDQAQV
VISMLPASRH VEGLYLGEDG LLARLPAGTL VIECSTIAPE SARKVHAAAR ERGVALLDAP
VSGGTAGAAA GTLTFMVGGE AQALEKARPI LAAMGRNIFH AGPDGAGQVA KVCNNQVLAV
QMIATAEAMA MGVANGLEPA VLAEIMRQSS GGNWTLEKYN PWPGVMENAP ASKGYSGGFM
AELMAKDLGL AQETASHSGN STPMGALALQ LYRLLLKQGK GKQDFSVVQQ LFVQ
//
