(data stored in SCRATCH zone)

SWISSPROT: D1CDW2_THET1

ID   D1CDW2_THET1            Unreviewed;       566 AA.
AC   D1CDW2;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, 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=Tter_0196 {ECO:0000313|EMBL:ACZ41118.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41118.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41118.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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; CP001825; ACZ41118.1; -; Genomic_DNA.
DR   RefSeq; WP_012874153.1; NC_013525.1.
DR   STRING; 525904.Tter_0196; -.
DR   EnsemblBacteria; ACZ41118; ACZ41118; Tter_0196.
DR   KEGG; ttr:Tter_0196; -.
DR   eggNOG; ENOG4105C01; Bacteria.
DR   eggNOG; COG0129; LUCA.
DR   HOGENOM; HOG000173155; -.
DR   KO; K01687; -.
DR   OMA; PFGRYVM; -.
DR   OrthoDB; 193579at2; -.
DR   BioCyc; TTER525904:G1GGS-199-MONOMER; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   Proteomes; UP000000323; Chromosome 1.
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; D1CDW2.
DR   SWISS-2DPAGE; D1CDW2.
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:UP000000323};
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:ACZ41118.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00012,
KW   ECO:0000256|SAAS:SAAS00943828};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323}.
FT   METAL       130    130       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00012}.
FT   METAL       202    202       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00012}.
SQ   SEQUENCE   566 AA;  59666 MW;  100AAB71BDD0F9AD CRC64;
     MSDASTGFDP RHKSRTIVEG RERAGARSML RAIGWTDEDF HKPVIGVAHC WIETMPCNYG
     HRELAEHVKR GIRDAGAVPV EVNTVAISDG ITMGTEGMKA SLISREVIAD SIELVGRGHM
     FDAMVILVAC DKTIPAGAMA LARLDIPGFL IYTGTIYPGK YKGRDVNIQD VYEAIGAAAA
     GKITDEELTE LEKVACPGIG ACGGQYTANT MATVIEALGI APVGSGSTPQ PHPDKKRICY
     EAGKLVVDQL KRGLKPSDIL TRQAFLNGIA AATGTGGSTN AVLHLLAIAR EAGVELTIDD
     FNEISENTPV ITDLRPSGKY TAVDVYEAGG IELILKRLIE GGKIDGSQLT PTGRTLAEEV
     ANVQERKPGQ QVILSLDNPK SPVGGLVILK GNLAPEGAVV KIAASGRTYH KGPARVFDCE
     EDAMDAVINK QINPGDVVVI RYEGPKGGPG MREMLGVTSA IVGEGLGDSV ALLTDGRFSG
     ATRGLMVGHV SPEAAVGGPI AALREGDIVT IDLDNKKLEV DLPQEVITAR MQEWKAPAPR
     YTSGVFAKYA ALVSSASEGA VTKAFL
//

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