ID A0A093ZRU8_9PEZI Unreviewed; 1350 AA.
AC A0A093ZRU8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 31.
DE RecName: Full=dihydroxy-acid dehydratase {ECO:0000256|ARBA:ARBA00029490};
DE EC=4.2.1.9 {ECO:0000256|ARBA:ARBA00029490};
GN ORFNames=V492_00421 {ECO:0000313|EMBL:KFY17753.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY17753.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY17753.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY17753.1,
RC ECO:0000313|Proteomes:UP000029299};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate
CC + H2O; Xref=Rhea:RHEA:24809, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:49072; EC=4.2.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00029304};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24810;
CC Evidence={ECO:0000256|ARBA:ARBA00029304};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 3/4.
CC {ECO:0000256|ARBA:ARBA00029437}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 3/4. {ECO:0000256|ARBA:ARBA00029436}.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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:KFY17753.1}.
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DR EMBL; JPJU01000079; KFY17753.1; -; Genomic_DNA.
DR STRING; 1420902.A0A093ZRU8; -.
DR HOGENOM; CLU_002425_1_0_1; -.
DR UniPathway; UPA00047; UER00057.
DR UniPathway; UPA00049; UER00061.
DR Proteomes; UP000029299; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR HAMAP; MF_00012; IlvD; 1.
DR InterPro; IPR042096; Dihydro-acid_dehy_C.
DR InterPro; IPR004404; DihydroxyA_deHydtase.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR InterPro; IPR037237; IlvD/EDD_N.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; TIGR00110; ilvD; 1.
DR PANTHER; PTHR21000; DIHYDROXY-ACID DEHYDRATASE DAD; 1.
DR PANTHER; PTHR21000:SF5; DIHYDROXY-ACID DEHYDRATASE, MITOCHONDRIAL; 1.
DR Pfam; PF00920; ILVD_EDD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
DR PROSITE; PS00887; ILVD_EDD_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029299}.
FT DOMAIN 374..698
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1350 AA; 147392 MW; 9BF056D0D17CBE1C CRC64;
MTDQNHHIPD PHSEEDNHSE KDSAAHHLIR LNESLNIQND THEVKALQRH APDDLVFTSM
TIAPSPPPPT VCAPPNSRAT LSSLNTSQQR HTGASSSESS PVSATRLRVQ RSFTSRPSEP
ERSDSNQERR ATKAIPIART PSIKQVLASS VGSNSYTGSA PNSALSSPQL NAMPDLTPLP
SPIMSNDSPG PWRRRISRSE YNESRTAPLT GDTALVTPSG ELIPSAIANE SKRRAYHGLL
NSEEIAFKPS NYKREKQTPT HSRNRSMSEY TPDPQTPRKR QQSVSGTYPK DNLPDRAPPV
DSHMRREPNL ALQRGIAPVP RPPTPPSSRT GGESSESDSA TSNAVKPMAR DSKKKSKPIY
FDAVTIASNE KRRWRALKLL GEGTFSKVVL ATSQLEKDSN MVDEEDDISL PDNEATESAL
TESDTKKLVA VKICEHGPKG GASEERVEIS LKRELELMKS IHHPSLVDLQ AWNMEESRAI
LVLGYCPGGD LFEVASQRPL ILVPSLLQRI FAEIVFAIQY LHERRIVHRD IKLENVLVNL
PYSELAKPTD WSTYPYSVIT VTDLGLARYV TDDEKLSTRC GSDDYAAPEV IMGQPYDGRA
VDAWSLGVLL YALLESRLPF DPNPGLSEGH KQRSRTSHRI ARVEWRWLTW EGDDGDHEAD
EAKFEAAGLK TAMEITENLL KRARSRWTVD RVAQLEWVTS AIQVDGGIRF RNEEEDRIGS
NSDNSCSVTQ LNVEQWLVLQ LPRERYTFES PSPLQLKSGT ACRSLSSAQP LRNATPKDSE
RQLNKTSATI TQPKSQGASQ AMLYATGMDE ERLNKAQVGI SSVWHSGNPC NMHLLDLNHR
VKEGVERAGL VGYQFNTIGV SDGISMGTTG MRYSLQSRDL IADSIETVMG GQWYDANISI
PGCDKNMPGV MMAMGRVNRP SLMVYGGSIK PGCSATQGNA DIDIVSAFQA YGQFITGEIT
EEVRYDIIRN ACPGGGACGG MYTANTMATA IEVMGMTLPG SSSNPAESKA KYLECLAAGG
AIKTLLQEDI RPSDILTRQA FENAMIVVII TGGSTNAVLH LIAIADSVGI KLTIDDFQAV
SDRIPFLADL KPSGKYVMAD LHNIGGTPSL LKFLLKEGLI DGSGMTVTGK TLAKNLEAFP
EFPTDQTIIR PISNPIKETG HIQILYGSLA PGGSVGKITG KEGLTFTGKA RVYDAENLFI
EALERGEIKK GEKTVVVIRY EGPKGGPGMP EMLKPSSAIM GAGLGKDCAL ITDGRFSGGS
HGFLIGHVVP EAQEGGPIAL VRDGDEITID AETKKMDLNV SETELAERRK TWVEPPLKYK
KGTLAKYARL VSDASRGCIT DGAMDENQKR
//
