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ILVD_BUCAP
ID   ILVD_BUCAP              Reviewed;         617 AA.
AC   O51887;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 124.
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=BUsg_576;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9516544; DOI=10.1007/pl00006760;
RA   Clark M.A., Baumann L., Baumann P.;
RT   "Sequence analysis of a 34.7-kb DNA segment from the genome of Buchnera
RT   aphidicola (endosymbiont of aphids) containing groEL, dnaA, the atp operon,
RT   gidA, and rho.";
RL   Curr. Microbiol. 36:158-163(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: Functions in the biosynthesis of branched-chain amino acids.
CC       Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate
CC       (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-
CC       3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-
CC       dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate),
CC       the penultimate precursor to L-isoleucine and L-valine, respectively.
CC       {ECO:0000255|HAMAP-Rule:MF_00012}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00012};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24810;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00012};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2-
CC         oxopentanoate + H2O; Xref=Rhea:RHEA:27694, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:35146, ChEBI:CHEBI:49258; EC=4.2.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00012};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27695;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00012};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00012};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis
CC       acid cofactor. {ECO:0000255|HAMAP-Rule:MF_00012};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={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   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00012}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000255|HAMAP-
CC       Rule:MF_00012}.
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DR   EMBL; AF008210; AAC38125.1; -; Genomic_DNA.
DR   EMBL; AE013218; AAM68110.1; -; Genomic_DNA.
DR   RefSeq; WP_011054076.1; NC_004061.1.
DR   AlphaFoldDB; O51887; -.
DR   SMR; O51887; -.
DR   STRING; 198804.BUsg_576; -.
DR   EnsemblBacteria; AAM68110; AAM68110; BUsg_576.
DR   KEGG; bas:BUsg_576; -.
DR   eggNOG; COG0129; Bacteria.
DR   HOGENOM; CLU_014271_4_2_6; -.
DR   OMA; TQGRNMA; -.
DR   OrthoDB; 193579at2; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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;
KW   2Fe-2S; Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Iron; Iron-sulfur; Lyase; Magnesium; Metal-binding.
FT   CHAIN           1..617
FT                   /note="Dihydroxy-acid dehydratase"
FT                   /id="PRO_0000103447"
FT   ACT_SITE        517
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT   BINDING         81
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT   BINDING         122
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT   BINDING         123
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT   BINDING         124
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT   BINDING         195
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT   BINDING         491
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
FT   MOD_RES         124
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00012"
SQ   SEQUENCE   617 AA;  67860 MW;  59A52ECDBDFC9381 CRC64;
     MPKYRSFTTT HGRNMSGARS LWRATGMTDE DFKKPIIAIV NSFSQFVPGH IHLQEVGKII
     SKEIKKYGGV PKEFNTIAID DGIAMGHSGM LYSLPSRELI ADSIEYVINA HCVDSMICVS
     NCDKITPAMF MASLRLNIPS VFVSGGPMEA GKIKTKDKTK KIDLVDAIIH GGDSNKSDDF
     IREIELSACP TCGSCSGMFT ANSMNCLIEA IGLSLPGNGT LLATHIDRKK LFKKSARNIV
     KITKDYYLNN NKNVLPRNIA NKESFENAMA LDIAMGGSTN TILHLLAAAY EGKVDFKMSD
     INNLSKKIPH ICKVAPSTNL YHVEDVHRAG GVMRILGELN RSNLLNKKTE NILGLNLEKT
     LKKYDILSTK NKNVIKMFHA GPGGNRTIKP FSQNYRWNKL DKDRVNGCIR SHENAYSKNG
     GLSVLYGNLA KNGCIIKTAS IDKKHYIFSG PAKVYESQEE AVSAILSGKI IAGDVIVIRY
     EGPKGGPGMQ EMLYPTTYLK SINLDKQCAL ITDGRFSGGT SGLSIGHISP EAANKGIIAL
     VENGDDIQIN IVNKTIHLNI TEKELNLRII KENAKGLKAY KPLNRKRNIS FALRAYAHFA
     LSADKGAIRN KKKLFNF
 
 
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