(data stored in ACNUC7421 zone)

SWISSPROT: ILVD_HISS2

ID   ILVD_HISS2              Reviewed;         611 AA.
AC   B0UW18;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   11-DEC-2019, entry version 67.
DE   RecName: Full=Dihydroxy-acid dehydratase {ECO:0000255|HAMAP-Rule:MF_00012};
DE            Short=DAD {ECO:0000255|HAMAP-Rule:MF_00012};
DE            EC=4.2.1.9 {ECO:0000255|HAMAP-Rule:MF_00012};
GN   Name=ilvD {ECO:0000255|HAMAP-Rule:MF_00012}; OrderedLocusNames=HSM_0213;
OS   Histophilus somni (strain 2336) (Haemophilus somnus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=228400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2336;
RG   US DOE Joint Genome Institute;
RA   Siddaramappa S., Duncan A.J., Challacombe J.F., Rainey D., Gillaspy A.F.,
RA   Carson M., Gipson J., Gipson M., Bruce D., Detter J.C., Han C.S., Land M.,
RA   Tapia R., Thompson L.S., Orvis J., Zaitshik J., Barnes G., Brettin T.S.,
RA   Dyer D.W., Inzana T.J.;
RT   "Complete sequence of Haemophilus somnus 2336.";
RL   Submitted (FEB-2008) 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:0000255|HAMAP-
CC         Rule:MF_00012};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00012};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00012};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 3/4. {ECO:0000255|HAMAP-
CC       Rule:MF_00012}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00012}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000255|HAMAP-
CC       Rule:MF_00012}.
DR   EMBL; CP000947; ACA31836.1; -; Genomic_DNA.
DR   RefSeq; WP_012341084.1; NC_010519.1.
DR   SMR; B0UW18; -.
DR   PRIDE; B0UW18; -.
DR   EnsemblBacteria; ACA31836; ACA31836; HSM_0213.
DR   GeneID; 31486492; -.
DR   KEGG; hsm:HSM_0213; -.
DR   HOGENOM; HOG000173155; -.
DR   KO; K01687; -.
DR   OMA; IPGHVHL; -.
DR   OrthoDB; 193579at2; -.
DR   BioCyc; HSOM228400:G1GB8-219-MONOMER; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   Proteomes; UP000008543; 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; B0UW18.
DR   SWISS-2DPAGE; B0UW18.
KW   4Fe-4S; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome.
FT   CHAIN           1..611
FT                   /note="Dihydroxy-acid dehydratase"
FT                   /id="PRO_1000073979"
FT   METAL           122
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT   METAL           195
FT                   /note="Iron-sulfur (4Fe-4S)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
SQ   SEQUENCE   611 AA;  65432 MW;  A09BE93F9FF55083 CRC64;
     MPKLRSATST QGRNMAGARA LWRATGMKEN DFGKPIIAVV NSFTQFVPGH VHLKDMGQLV
     AAEIEKFGGV AKEFNTIAVD DGIAMGHGGM LYSLPSRDLI ADSVEYMVNA HCADAMVCIS
     NCDKITPGML MAALRLNIPT VFVSGGPMEA GKTKLSDQII KLDLVDAMIQ GANPNVSDDV
     SEQIERSACP TCGSCSGMFT ANSMNCLTEA LGLSLPGNGS CLATHADRKQ LFLAAGKQIV
     ELCKRYYEQD DTSVLPRSIA TKEAFDNAMS LDIAMGGSTN TVLHLLAAAQ EAEVNFTMAD
     IDRLSRVVPC LSKVAPNTQK YHMEDVHRAG GIMAILGELD RAGLLNSQTR TILGMSIGEQ
     IAKYDIKLTQ DKAIHKFFRA GPAGIRTTQA FSQDCRWDTV DDDRENGCIR SKEFAYSQDG
     GLAMLSGNIA LDGCIVKTAG VDESILKFSG KAIVFESQED AVSGILGGKV QAGHVVVIRY
     EGPKGGPGMQ EMLYPTSYLK SMGLGKACAL LTDGRFSGGT SGLSIGHCSP EAAAGGLIGV
     VKDGDIIEID IPNRRIELMV SEEELAERRA EQDKLGWKPA NRQREVSFAL KVYGYFATSA
     DKGAVRDKTK I
//

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