ID A0A1H3GZ79_9ACTN Unreviewed; 307 AA.
AC A0A1H3GZ79;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN05661080_02253 {ECO:0000313|EMBL:SDY08245.1};
OS Modestobacter sp. DSM 44400.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=1550230 {ECO:0000313|EMBL:SDY08245.1, ECO:0000313|Proteomes:UP000199500};
RN [1] {ECO:0000313|EMBL:SDY08245.1, ECO:0000313|Proteomes:UP000199500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44400 {ECO:0000313|EMBL:SDY08245.1,
RC ECO:0000313|Proteomes:UP000199500};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNOZ01000014; SDY08245.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3GZ79; -.
DR STRING; 1550230.SAMN05661080_02253; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000199500; 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:UP000199500}.
FT DOMAIN 8..166
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 169..294
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 175
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 307 AA; 30095 MW; 6E5420442D769C10 CRC64;
MTETPRAVGF IGLGNMGGPM AANLVAAGHA VTGFDLSPEA NDAARAAGVP IAGSAAEAVA
SAEYVITMLP AGRHVLGAYQ GEDGLLAAAP AGTLFIDCST IDVADARTAA AAAQAAGHRA
IDAPVSGGVA GASAGTLTFM VGGSEEDIEA AEPLLTVMGR KTVHCGGPGA GQAAKLCNNM
ILGISMIAVS EAFVLGEALG LSNQALFDVS STATGQCWAL TTNCPVPGPV PASPANRDYQ
AGFAAALMAK DLGLAADAVT SNGVQATLGL AAADIYRQLA DGELAGQDFS TVINRIRGNS
GAGAADA
//
