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Database: UniProt
Entry: A0A1I2QI49_9CORY
LinkDB: A0A1I2QI49_9CORY
Original site: A0A1I2QI49_9CORY 
ID   A0A1I2QI49_9CORY        Unreviewed;       308 AA.
AC   A0A1I2QI49;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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=SAMN05660282_00439 {ECO:0000313|EMBL:SFG27293.1};
OS   Corynebacterium spheniscorum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=185761 {ECO:0000313|EMBL:SFG27293.1, ECO:0000313|Proteomes:UP000199065};
RN   [1] {ECO:0000313|EMBL:SFG27293.1, ECO:0000313|Proteomes:UP000199065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J11, PG 39 {ECO:0000313|Proteomes:UP000199065};
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; FOPJ01000002; SFG27293.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2QI49; -.
DR   STRING; 185761.SAMN05660282_00439; -.
DR   OrthoDB; 3185659at2; -.
DR   UniPathway; UPA00362; -.
DR   Proteomes; UP000199065; 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:UP000199065}.
FT   DOMAIN          17..172
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          175..302
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   ACT_SITE        181
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ   SEQUENCE   308 AA;  32371 MW;  06A25151491F37C9 CRC64;
     MSTPHDPNRL SAQEPALAFI GLGHMGLPMA TNLAKAGLKV SGFDVVEEAC EKARGNGIDA
     SADLTKAVEG ATVVWTMLPN GDLVRDTITK AMELLPEGTL FIDSSTISVV DAQELGKLTS
     EKGYYFIDAP VSGGVVGASA GTLAFMVGGG EDAIQRAYPL LDILGGSITH CGAVGSGQTV
     KICNNLVLGV QQIVVAESMI LADRLGIDPK TYMEVVSNST GSCWALTKNC PVPGPVPESP
     ANHDYQPGYA SALMLKDLRL AKEVLEQTGT TANMGMQAWQ MYETFCEQGN AGLDFSAIIR
     LIDEKKDG
//
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