GenomeNet

Database: UniProt
Entry: M7SVW0_EUTLA
LinkDB: M7SVW0_EUTLA
Original site: M7SVW0_EUTLA 
ID   M7SVW0_EUTLA            Unreviewed;       646 AA.
AC   M7SVW0;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=3-hydroxyisobutyrate dehydrogenase {ECO:0000256|ARBA:ARBA00012991};
DE            EC=1.1.1.31 {ECO:0000256|ARBA:ARBA00012991};
GN   ORFNames=UCREL1_4352 {ECO:0000313|EMBL:EMR68633.1};
OS   Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS   armeniacae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX   NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR68633.1, ECO:0000313|Proteomes:UP000012174};
RN   [1] {ECO:0000313|Proteomes:UP000012174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX   PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA   Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT   "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT   EL1.";
RL   Genome Announc. 1:E0022813-E0022813(2013).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KB706202; EMR68633.1; -; Genomic_DNA.
DR   RefSeq; XP_007792274.1; XM_007794083.1.
DR   AlphaFoldDB; M7SVW0; -.
DR   STRING; 1287681.M7SVW0; -.
DR   KEGG; ela:UCREL1_4352; -.
DR   eggNOG; KOG0409; Eukaryota.
DR   HOGENOM; CLU_443534_0_0_1; -.
DR   OMA; CWADELG; -.
DR   OrthoDB; 203032at2759; -.
DR   Proteomes; UP000012174; 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   CDD; cd07730; metallo-hydrolase-like_MBL-fold; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
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   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
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; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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:UP000012174}.
FT   DOMAIN          317..495
FT                   /note="6-phosphogluconate dehydrogenase NADP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF03446"
FT   DOMAIN          512..638
FT                   /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF14833"
FT   REGION          199..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  68060 MW;  53B623FBFA69DD51 CRC64;
     MTATTDPKPP VFVTVSALDA GHLTLPERLF ITDADPEKSN TVPSLSFLIQ HPSPSPSREG
     SQTTNLVFDL GIKRDLDRYT PSQQIHTAQR QPVITDPDCA ASLRYGVPGK GKPKPKKDEV
     LLDPSKDIDL VIISHVHWDH VGTPSDFSSA TFAVGSGTLD LLRNGAGHLY PADLFDEDEL
     PRTRTVEFPV VPGATEYADG SDIPTHTATP ENSEAKLPPS ASQWSWGRLG GFPNALDLFG
     DGSVYVIDSP GHLYGHVNLL TRISEAKYVY LGGDCCHDTR ILSGKSDIAM YGDGKGGLRS
     VHVDTNAAKK TLDRIRAFVS LGVMGYPMAK NLRVGLGPET TLLICDVNTE AIARFQKETE
     GQGPVSVVTN GFEAVKAANT VITMLPGSAA VKAVYLDPGT GVLAGAVAAA AENGSGNALL
     PPKLIMECGT IETDTITSVA EAAQATSAAK LHSTLTFVDA PVSGGPMGAQ AGTLTFMVGC
     QPAASAQIFP VVKSYLRHMG NADGIFLCGD VGAGTAFKII NNYLSAITSL AASEALNIGV
     KAGLDPKLLT DVINGSGGQC WVTSKSNPVP GVQDNVPSSR GYEGGFRIEL CAKVLGMGSR
     LAETVGARTV LDRPTLDAFG EAIADERYAG KDARVVYKWL NDSERK
//
DBGET integrated database retrieval system