ID A0A094GWB3_9PEZI Unreviewed; 1807 AA.
AC A0A094GWB3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 32.
DE RecName: Full=dihydroxy-acid dehydratase {ECO:0000256|ARBA:ARBA00029490};
DE EC=4.2.1.9 {ECO:0000256|ARBA:ARBA00029490};
GN ORFNames=V498_00110 {ECO:0000313|EMBL:KFZ00391.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFZ00391.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFZ00391.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
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:KFZ00391.1}.
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DR EMBL; JPKA01000011; KFZ00391.1; -; Genomic_DNA.
DR HOGENOM; CLU_002425_0_0_1; -.
DR UniPathway; UPA00047; UER00057.
DR UniPathway; UPA00049; UER00061.
DR Proteomes; UP000029270; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 818..1140
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 438..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1807 AA; 198176 MW; 9EABF302945DDFE4 CRC64;
MEKYSQFRDR GSGIAPFFPV TSPTSTLYLP VNIFLFAVKL PLFLAITVAY FFFLQWLPLG
AFIRKAMLWV ILGAPGIWWI DLQIDGVKKG SLAREKQRLP APSSIIASSF TSPVDALYLA
AIFDPVFTVS YPGTRQVRPI SLLGAMLRAL SGPEEAPPAG VKLVDLGTLV SENPDSIIVV
FPECTTTNGK GILPLSPSLL AVPSTTKIFP INLRYSPPDI TTPVPGRYWS FLWNLLSQQT
HCIRVRIAEA VYNTAKPVDV SSEKKDKYLD NFLDLSGEDS TDLSSGIRKR GVNAEEQKVL
DQVGEALARL GRVKRVGLAV KDKAAFCVGS LYIYRTLTIR KEVLEEPRQK GGQPVAQYLY
ILSPVASESF CDSDLQPPSY IRTTLQRRPI VPSDQKKEVK VKSNFLRTDL HDLRYTPLQL
PQKLHALKTM LLGRPHRGAT MTNPNHHIPG PHSEEDNDSE RRNFVGQHLK GLDEPLNTQN
DTHIKALKAL PRREPEDLVF TSTTIAPSPP PPIVCAPSNS RATLSPLNTT QQRHSGASSS
DSSPVSATRL RVQRSFTSRP TELDASDSNQ ERRTSKPIPI ARTPSIKQVL ASSLGSNSYA
GSAPNSALSS PQLNAMPDLT PLPSPIMSND SPGPWRRRIS RSEYNESRTA PLTGDTALVT
PTGELIPSAI ANESKRRAYH GLLLNSEDAP LKPSNYKREM QNSSHSRNRS MSEYTPDPQT
PRNRQQSVSG SYPKDMLPDR APPVDSLMRR EPHLALQRGI APVPRPPTPP SSRTGGESSE
SDSAASTVVK PMTKDYKKRS KHIYFDAVTI ANNKKRRWRA LKLLGEGTFS KVVLATSQLE
DSNTVVEDDV SLPDNEATED ALTEADTKKL VAVKICEHGP KGGASEERVE ISLKRELELM
KSIHHPSLVE LQAWSMEESR AILVLGYCPG GDLFEVASQR PSILVPSLLQ RIFAEIVFAI
QYLHERHIVH RDIKLENVLV NLPHSELEKP IDWSTYPYSV ITVTDLGLAR YVTDDEKLST
RCGSDDYAAP EVIMGQPYDG RAVDAWSLGV LLYALLESRL PFDPNPGLSE GHKQRSRTSH
RIARVEWRWV MWEGEDGDHE ADEAKFEAAG LKTAMEITEN LLKRARSRWT VDRVAQIEWV
KSAIQVEGGI KFRSEEEVGK AETNDLAIDK ESKVWHDLFD TKGRFLEALS FESITVMHAR
LRIRANARVL NYPRAPNYVR SLSSAQPLRN ATPKDSERQL NKISATITQP KSQGASQAML
YATGMTEERL NKAQVGISSV WHSGNPCNMH LLDLNNRVKE GVERAGLVGY QFNTIGVSDG
ISMGTTGMRY SLQSRDLIAD SIETVMGGQW YDANISIPGC DKNMPGVMMA MGRVNRPSLM
VYGGSIKPGC SATQGNADID IVSAFQAYGQ FITGEITEEV RYDIIRHACP GGGACGGMYT
ANTMATAIEV MGMTLPGSSS NPAESKAKHL ECLAAGGAIK TLLQEDIRPS DILTRQAFEN
AMIVVIITGG STNAVLHLIA IADSVGIKLT IDDFQAVSDR IPFLADLKPS GKYVMADLHN
IGGTPSLLKF LLKEGLIDGT GMTVTGKTLA KNLEAFPEFP TDQTIIRPLS NPIKETGHIQ
ILRGSLAPGG SVGKITGKEG LTFTGKAKVY DAESLFIEAL ERGEIKKGDK TVVVIRYEGP
KGGPGMPEML KPSSAIMGAG LGKDCALVTD GRFSGGSHGF LIGHVVPEAQ EGGPIGLVRD
GDEITIDAES KRMDLNVSEQ ELAERRKTWV APPLKYKKGT LAKYARLVSD ASRGCITDGE
MDENQQR
//
