ID A0A1C1C8J2_9EURO Unreviewed; 358 AA.
AC A0A1C1C8J2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=3-hydroxyisobutyrate dehydrogenase {ECO:0000256|ARBA:ARBA00012991};
DE EC=1.1.1.31 {ECO:0000256|ARBA:ARBA00012991};
GN Name=Hibadh {ECO:0000313|EMBL:OCT44781.1};
GN ORFNames=CLCR_05922 {ECO:0000313|EMBL:OCT44781.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT44781.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) 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|ARBA:ARBA00000062};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC {ECO:0000256|ARBA:ARBA00005109}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC dehydrogenase subfamily. {ECO:0000256|ARBA:ARBA00006013}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OCT44781.1}.
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DR EMBL; LGRB01000020; OCT44781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1C8J2; -.
DR STRING; 86049.A0A1C1C8J2; -.
DR VEuPathDB; FungiDB:CLCR_05922; -.
DR VEuPathDB; FungiDB:G647_07456; -.
DR eggNOG; KOG0409; Eukaryota.
DR Proteomes; UP000094526; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:UniProtKB-KW.
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; IPR029154; HIBADH-like_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000094526}.
FT DOMAIN 37..225
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 228..354
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
SQ SEQUENCE 358 AA; 38176 MW; C0CE09F0269B2D3B CRC64;
MIVPSMSSAL RQAACSQSFR VSVRHFSQTA TRDASWGFIG LGAMGYPMAK NLRAKIPEGD
MLTIFDLNKA SLEQFTQEAT PSGVVVAKSP REVAEKSFNS SSIVTICCTL GLTGVRQDHI
ISALPEPRHV KGVFEEILAS PLPKPPSESS RLFIDCSTID PTTSREVAKL VKEKAGAGFV
DAPMSGGVVG ARAGTLTFMV GGEKEDMPKI QEILLLMGKK VWHMGPQGTG LSGKLANNYA
LAINNIACAE AMNLGMRWGI EGKALADLLN SATGRSWPSE INNPVPGVLE SSPATRGYEG
GFGVSLMNKD LRLAMTAAQE AGAKLVLAEK AKEVYDSTEK AHKGKDFSVV YRWLGGKV
//
