ID Q5X094_LEGPL Unreviewed; 298 AA.
AC Q5X094;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 126.
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=lpl0127 {ECO:0000313|EMBL:CAH14357.1};
OS Legionella pneumophila (strain Lens).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245 {ECO:0000313|EMBL:CAH14357.1, ECO:0000313|Proteomes:UP000002517};
RN [1] {ECO:0000313|EMBL:CAH14357.1, ECO:0000313|Proteomes:UP000002517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens {ECO:0000313|EMBL:CAH14357.1,
RC ECO:0000313|Proteomes:UP000002517};
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Bruggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(2004).
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; CR628337; CAH14357.1; -; Genomic_DNA.
DR RefSeq; WP_011214407.1; NC_006369.1.
DR AlphaFoldDB; Q5X094; -.
DR KEGG; lpf:lpl0127; -.
DR LegioList; lpl0127; -.
DR HOGENOM; CLU_035117_6_0_6; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000002517; 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: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..291
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 298 AA; 31392 MW; 90EDAE3BB93674E8 CRC64;
MANIGFVGLG HMGFPMAINL LKAGHSVMGY DLQQSALEHF AEQGGAIAHN LQELAKGKDV
IVTMLQTGQQ VLHVCLGVDG IFSQLNAGSL YIDCSTIDVK SSRETHQIAK ENHLLVVDAP
VSGGVAGAAA ATLTFMVGGE AEDYNAAHPI LSAMGKKIIH TGGAGSGQAA KICNNMILGT
TMIAISEAFI LAKELGLSDG KLFEVVNNSS GQCWAMSKYV PVPGILENVP ANNDYKPGFA
ANMMLKDLLL SQNTAQSVHI ETPLGAKTTE IYQQFVDQGL GDIDFSAIIK HIGKTQEV
//
