(data stored in SCRATCH3701 zone)

SWISSPROT: D5E9T6_METMS

ID   D5E9T6_METMS            Unreviewed;       553 AA.
AC   D5E9T6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 52.
DE   RecName: Full=Dihydroxy-acid dehydratase {ECO:0000256|HAMAP-Rule:MF_00012};
DE            Short=DAD {ECO:0000256|HAMAP-Rule:MF_00012};
DE            EC=4.2.1.9 {ECO:0000256|HAMAP-Rule:MF_00012};
GN   Name=ilvD {ECO:0000256|HAMAP-Rule:MF_00012};
GN   OrderedLocusNames=Mmah_0405 {ECO:0000313|EMBL:ADE35937.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35937.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35937.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate +
CC         H2O; Xref=Rhea:RHEA:20936, ChEBI:CHEBI:11424, ChEBI:CHEBI:11851,
CC         ChEBI:CHEBI:15377; EC=4.2.1.9; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00012};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00012};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00012};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 3/4. {ECO:0000256|HAMAP-
CC       Rule:MF_00012}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 3/4. {ECO:0000256|HAMAP-Rule:MF_00012}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000256|HAMAP-
CC       Rule:MF_00012}.
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DR   EMBL; CP001994; ADE35937.1; -; Genomic_DNA.
DR   RefSeq; WP_013036880.1; NC_014002.1.
DR   EnsemblBacteria; ADE35937; ADE35937; Mmah_0405.
DR   GeneID; 8982540; -.
DR   KEGG; mmh:Mmah_0405; -.
DR   eggNOG; arCOG04045; Archaea.
DR   eggNOG; COG0129; LUCA.
DR   HOGENOM; HOG000173155; -.
DR   KO; K01687; -.
DR   OMA; IPGHVHL; -.
DR   OrthoDB; 7176at2157; -.
DR   BioCyc; MMAH547558:G1GHT-402-MONOMER; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.30.80; -; 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   Pfam; PF00920; ILVD_EDD; 1.
DR   SUPFAM; SSF143975; SSF143975; 1.
DR   TIGRFAMs; TIGR00110; ilvD; 1.
DR   PROSITE; PS00886; ILVD_EDD_1; 1.
DR   PROSITE; PS00887; ILVD_EDD_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E9T6.
DR   SWISS-2DPAGE; D5E9T6.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00012};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00012};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00012};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00012};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00012};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00012, ECO:0000313|EMBL:ADE35937.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           119
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
FT   METAL           191
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00012"
SQ   SEQUENCE   553 AA;  59255 MW;  94D8150E4EACEC4F CRC64;
     MRSDSIKKGT ERAPNRSLLR ATGVTDSEME KPFIAVVNSW TEVVPGHIHL DKVSEAVKAG
     IRNAGGVPFE FNTIGICDGI AMGHEGMKYS LPSREVIEDS IELMLEGHRL DGMVMITSCD
     KITPGHLMAA GRLDIPTIVV TGGPMLPGFS GDEPRDLVSV FEGIGEHRTG KATDEQLKVL
     ENVSCAGAGS CAGMFTANTM ACMTEALGLS LPGCATAHAV DAKKIHIAKE SGERIMALVD
     EGLSARKVVS QKSFENAIMV DMAVGGSTNT ALHLPAIAHA FDMELPLDTF DRLGRSIPHL
     IGLRPGGKYH MIDFERAGGV HAIMQRLRSK INRGEKTVTG KTVGENIDEY VIINPAINKK
     IIQTLEKPLH QEGGLAILKG NLAPEGGVVK QAAVEPAMMQ HKGPARVFES EEEAMHAILD
     NDIKPGDVVV IRYEGPKGGP GMREMLSPTS AIAGMGLADS VALITDGRFS GGTRGPCIGH
     ISPEAMEGGP IGLIEEGDMI EIDIPARKLE LLIDEEEMQK RKENFKPLVK EVKGYLARYR
     KSVSSANKGA IRE
//

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