ID I1RMT6_GIBZE Unreviewed; 333 AA.
AC I1RMT6; A0A098DWK8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=3-hydroxyisobutyrate dehydrogenase {ECO:0000256|ARBA:ARBA00012991, ECO:0000256|RuleBase:RU910714};
DE Short=HIBADH {ECO:0000256|RuleBase:RU910714};
DE EC=1.1.1.31 {ECO:0000256|ARBA:ARBA00012991, ECO:0000256|RuleBase:RU910714};
GN Name=FG05284.1 {ECO:0000313|EnsemblFungi:CEF86221};
GN ORFNames=FGRAMPH1_01T17529 {ECO:0000313|EMBL:CEF86221.1};
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533 {ECO:0000313|EMBL:CEF86221.1, ECO:0000313|Proteomes:UP000070720};
RN [1] {ECO:0000313|EnsemblFungi:CEF86221, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF86221};
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2] {ECO:0000313|EnsemblFungi:CEF86221, ECO:0000313|Proteomes:UP000070720}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF86221};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3] {ECO:0000313|EMBL:CEF86221.1, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1
RC {ECO:0000313|EMBL:CEF86221.1};
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4] {ECO:0000313|EnsemblFungi:CEF86221}
RP IDENTIFICATION.
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF86221};
RG EnsemblFungi;
RL Submitted (JAN-2017) to UniProtKB.
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 ECO:0000256|RuleBase:RU910714};
CC -!- PATHWAY: Amino-acid degradation; L-valine degradation.
CC {ECO:0000256|ARBA:ARBA00005109, ECO:0000256|RuleBase:RU910714}.
CC -!- SIMILARITY: Belongs to the HIBADH-related family. 3-hydroxyisobutyrate
CC dehydrogenase subfamily. {ECO:0000256|ARBA:ARBA00006013}.
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DR EMBL; HG970334; CEF86221.1; -; Genomic_DNA.
DR RefSeq; XP_011323795.1; XM_011325493.1.
DR AlphaFoldDB; I1RMT6; -.
DR STRING; 229533.I1RMT6; -.
DR EnsemblFungi; CEF86221; CEF86221; FGRRES_05284.
DR GeneID; 23552472; -.
DR KEGG; fgr:FGSG_05284; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G17529; -.
DR eggNOG; KOG0409; Eukaryota.
DR HOGENOM; CLU_035117_6_1_1; -.
DR InParanoid; I1RMT6; -.
DR OrthoDB; 203032at2759; -.
DR UniPathway; UPA00362; -.
DR Proteomes; UP000070720; Chromosome 3.
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:UP000070720}.
FT DOMAIN 26..195
FT /note="6-phosphogluconate dehydrogenase NADP-binding"
FT /evidence="ECO:0000259|Pfam:PF03446"
FT DOMAIN 198..326
FT /note="3-hydroxyisobutyrate dehydrogenase-like NAD-binding"
FT /evidence="ECO:0000259|Pfam:PF14833"
FT ACT_SITE 204
FT /evidence="ECO:0000256|PIRSR:PIRSR000103-1"
SQ SEQUENCE 333 AA; 35513 MW; 263DBACC8139D1BA CRC64;
MRPSTRLGSL MLRRGFASSA RRLDNYGFIG LGQMGYQMAK NLQSKLKPSD KVSIFDINPE
SMKGLETEMK AASSGAQVEL AASAFDASKD ADTIITVLPE PQHVKGVYKS IITSSLPKKD
RVFIDCSTID PSTSRQVAKT VSSAGQGMFV DAPMSGGVVG ATAGTLTFML GASPSLVPRL
EPVLMLMGKK VLHCGEQGAG LSAKLANNYL LALNNIATAE AMNLGMQWGL DPKKLAGVIN
VSTGRCWPSE VNNPVAGVVE TAPANRDYRG GFGISLMKKD LRLAMVAAEE AGARMELAKT
AFAVYKAAEK EEKCQGRDFS VVYRYLGGKE EQS
//
