(data stored in SCRATCH zone)

SWISSPROT: C8W654_DESAS

ID   C8W654_DESAS            Unreviewed;       554 AA.
AC   C8W654;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=Dihydroxy-acid dehydratase {ECO:0000256|HAMAP-Rule:MF_00012, ECO:0000256|SAAS:SAAS00943824};
DE            Short=DAD {ECO:0000256|HAMAP-Rule:MF_00012};
DE            EC=4.2.1.9 {ECO:0000256|HAMAP-Rule:MF_00012, ECO:0000256|SAAS:SAAS00943824};
GN   Name=ilvD {ECO:0000256|HAMAP-Rule:MF_00012};
GN   OrderedLocusNames=Dtox_0589 {ECO:0000313|EMBL:ACV61509.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61509.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61509.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate
CC         + H2O; Xref=Rhea:RHEA:20936, ChEBI:CHEBI:11424,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15377; EC=4.2.1.9;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00012,
CC         ECO:0000256|SAAS:SAAS01115286};
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, ECO:0000256|SAAS:SAAS00943826}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 3/4. {ECO:0000256|HAMAP-Rule:MF_00012,
CC       ECO:0000256|SAAS:SAAS00943830}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000256|HAMAP-
CC       Rule:MF_00012, ECO:0000256|SAAS:SAAS00943829}.
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DR   EMBL; CP001720; ACV61509.1; -; Genomic_DNA.
DR   RefSeq; WP_015756228.1; NC_013216.1.
DR   STRING; 485916.Dtox_0589; -.
DR   EnsemblBacteria; ACV61509; ACV61509; Dtox_0589.
DR   KEGG; dae:Dtox_0589; -.
DR   eggNOG; ENOG4105C01; Bacteria.
DR   eggNOG; COG0129; LUCA.
DR   HOGENOM; HOG000173155; -.
DR   KO; K01687; -.
DR   OMA; IPGHVHL; -.
DR   OrthoDB; 193579at2; -.
DR   BioCyc; DACE485916:G1GFV-596-MONOMER; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   Proteomes; UP000002217; 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; C8W654.
DR   SWISS-2DPAGE; C8W654.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00012,
KW   ECO:0000256|SAAS:SAAS00943818};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00012,
KW   ECO:0000256|SAAS:SAAS00943821};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_00012, ECO:0000256|SAAS:SAAS00943815};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00012, ECO:0000256|SAAS:SAAS00943817};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00012,
KW   ECO:0000256|SAAS:SAAS00943822};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00012, ECO:0000256|SAAS:SAAS00943827,
KW   ECO:0000313|EMBL:ACV61509.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00012,
KW   ECO:0000256|SAAS:SAAS00943828};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   METAL       119    119       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00012}.
FT   METAL       191    191       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00012}.
SQ   SEQUENCE   554 AA;  58498 MW;  C98DC547D101D3D6 CRC64;
     MRSDAMKLGL EKAPHRSLFK ALGYTDQELA RPLIGVVNAQ NEIVPGHLHL DDIAEAVKAG
     IRMAGGTPIE FPAIAVCDGI AMNHTGMKYS LASRELIADS IEVMSIAHPF DGLVLIPSCD
     KIVPGMLMAA ARLNIPAIVV SGGPMLAGKI KGQHKSLTNV FEAVGSVRAG KMSEEELADL
     EEAACPGCGS CSGMFTANSM NCLTEVLGMA LPGNGTIPAV SAARRRLAKQ TGMQIMYLVK
     ENICPSDILT MDAFNNGLTV DMALGCSTNT ILHLPAIASE AGVIIDLELV NKTSERTPNL
     CKLSPAGPHF IEELDEAGGI PAVMAELSKH DLLNLNSRTV SGVTVGENIN GSRVLRRDII
     RNIEDPYSPS GGITVMRGNL APDGAVVKKS AVAPEMLVHR GPARVFNSEE ESMDAIMNQT
     IQKGDVVVIR YEGPRGGPGM REMLTPTATL AGLGLDKEVA LLTDGRFSGA TRGAAIGHVS
     PEAALGGVIA VIQDGDMIDI DIPNCRLNVD LTEAEIDERM KKLVIPEPKI TRGYLARYAK
     MVTSASTGAV LAKD
//

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