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Database: UniProt
Entry: H9NL36_BACTU
LinkDB: H9NL36_BACTU
Original site: H9NL36_BACTU 
ID   H9NL36_BACTU            Unreviewed;       431 AA.
AC   H9NL36;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   13-SEP-2023, entry version 41.
DE   RecName: Full=dihydroxy-acid dehydratase {ECO:0000256|ARBA:ARBA00029490};
DE            EC=4.2.1.9 {ECO:0000256|ARBA:ARBA00029490};
DE   Flags: Fragment;
GN   Name=ilvD {ECO:0000313|EMBL:AFF60370.1};
OS   Bacillus thuringiensis serovar poloniensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=180894 {ECO:0000313|EMBL:AFF60370.1};
RN   [1] {ECO:0000313|EMBL:AFF60370.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IEBC-T54 001 {ECO:0000313|EMBL:AFF60370.1};
RX   PubMed=23073664; DOI=10.1007/s10482-012-9800-5;
RA   Soufiane B., Baizet M., Cote J.C.;
RT   "Multilocus sequence analysis of Bacillus thuringiensis serovars
RT   navarrensis, bolivia and vazensis and Bacillus weihenstephanensis reveals a
RT   common phylogeny.";
RL   Antonie Van Leeuwenhoek 103:195-205(2013).
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}.
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DR   EMBL; JQ728624; AFF60370.1; -; Genomic_DNA.
DR   AlphaFoldDB; H9NL36; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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: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   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   NCBIfam; TIGR00110; ilvD; 1.
DR   PANTHER; PTHR43661; D-XYLONATE DEHYDRATASE; 1.
DR   PANTHER; PTHR43661:SF3; D-XYLONATE DEHYDRATASE YAGF-RELATED; 1.
DR   Pfam; PF00920; ILVD_EDD; 1.
DR   SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   PROSITE; PS00886; ILVD_EDD_1; 1.
DR   PROSITE; PS00887; ILVD_EDD_2; 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}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFF60370.1"
FT   NON_TER         431
FT                   /evidence="ECO:0000313|EMBL:AFF60370.1"
SQ   SEQUENCE   431 AA;  46018 MW;  4388E55F4DE4A3DF CRC64;
     ADSVETVVNA HWFDGMICIP NCDKITPGMM MAALRINIPT VFVSGGPMAA GKTSKGEVVD
     LSSVFEGVGA YQSGKISEEE LKDIEDHGCP SCGSCSGMFT ANSMNCLCEV LGLALPGNGS
     ILAIDPRREE LIKQAAEKLK ILIERDIKPR DIVTEEAIDD AFALDMAMGG STNTVLHTLA
     LAQEAGLDYD MSRIDAVSRR VPHLCKVSPA SNWHMEDIDR AGGISAILKE MSRKEGVLHL
     DRITATGQTL RENIAHAEIK DKEVIHSLEN PHSEEGGLRI LKGNLAKDGA VIKSGATEVK
     RFEGPCVIFN SQDEALAGIM LGKVKKGDVV VIRYEGPRGG PGMPEMLAPT SAIAGMGLGA
     DVALLTDGRF SGASRGISVG HISPEAAAGG TIALLEQGDI VCIDVEERLL EVRVSDEELD
     KRKKEWKRPE P
//
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