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Database: UniProt
Entry: A0A0W0U8N4_9GAMM
LinkDB: A0A0W0U8N4_9GAMM
Original site: A0A0W0U8N4_9GAMM 
ID   A0A0W0U8N4_9GAMM        Unreviewed;       299 AA.
AC   A0A0W0U8N4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=garR_1 {ECO:0000313|EMBL:SPX60739.1};
GN   Synonyms=garR_2 {ECO:0000313|EMBL:STX39710.1};
GN   ORFNames=Lfee_0237 {ECO:0000313|EMBL:KTD04149.1}, NCTC11978_02915
GN   {ECO:0000313|EMBL:STX39710.1}, NCTC12022_01472
GN   {ECO:0000313|EMBL:SPX60739.1};
OS   Legionella feeleii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=453 {ECO:0000313|EMBL:KTD04149.1, ECO:0000313|Proteomes:UP000054698};
RN   [1] {ECO:0000313|EMBL:KTD04149.1, ECO:0000313|Proteomes:UP000054698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-44C {ECO:0000313|EMBL:KTD04149.1,
RC   ECO:0000313|Proteomes:UP000054698};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000251942, ECO:0000313|Proteomes:UP000254033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC11978 {ECO:0000313|EMBL:STX39710.1,
RC   ECO:0000313|Proteomes:UP000254033}, and NCTC12022
RC   {ECO:0000313|EMBL:SPX60739.1, ECO:0000313|Proteomes:UP000251942};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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; LNYB01000009; KTD04149.1; -; Genomic_DNA.
DR   EMBL; UASS01000011; SPX60739.1; -; Genomic_DNA.
DR   EMBL; UGNY01000001; STX39710.1; -; Genomic_DNA.
DR   RefSeq; WP_058443457.1; NZ_UGNY01000001.1.
DR   AlphaFoldDB; A0A0W0U8N4; -.
DR   STRING; 453.Lfee_0237; -.
DR   PATRIC; fig|453.4.peg.259; -.
DR   OrthoDB; 9786703at2; -.
DR   UniPathway; UPA00362; -.
DR   Proteomes; UP000054698; Unassembled WGS sequence.
DR   Proteomes; UP000251942; Unassembled WGS sequence.
DR   Proteomes; UP000254033; 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};
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:UP000054698}.
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   299 AA;  31455 MW;  49B85A17056C7642 CRC64;
     MARIGFVGLG HMGLPMAINL VKAGHSVTGF DLQAKAVDAL VAAGGSKASS LPKAAQNQDV
     IITMLQTGKQ VRQVCLGEQG LFAHITPKAL YIDCSSIDVQ TSREIHQHAT IRHIQVIDAP
     VSGGVAGAAA ATLTFMVGGR EQAFEKAKPV LSAMGKKLIH TGAGGSGQAA KICNNMVLAI
     SMIGISEAFT LAEHLGLSHQ KLYEVVNSSS GQCWAMSQYV PVPNVLPNVP ANNAYQPGFT
     AAMMLKDLTL SQSTAAMVNV ETPMGAKAMA LYQKMNEKGL GHMDFSAIIK LIDQDKDED
//
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