ID ILVD_PROMP Reviewed; 559 AA.
AC Q7V1T1;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 01-MAY-2013, entry version 62.
DE RecName: Full=Dihydroxy-acid dehydratase;
DE Short=DAD;
DE EC=4.2.1.9;
GN Name=ilvD; OrderedLocusNames=PMM0774;
OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4).
OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59919;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1986 / MED4;
RX PubMed=12917642; DOI=10.1038/nature01947;
RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P.,
RA Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R.,
RA Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M.,
RA Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A.,
RA Webb E.A., Zinser E.R., Chisholm S.W.;
RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic
RT niche differentiation.";
RL Nature 424:1042-1047(2003).
CC -!- CATALYTIC ACTIVITY: 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-
CC oxobutanoate + H(2)O.
CC -!- COFACTOR: Binds 1 4Fe-4S cluster (Potential).
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 3/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC from pyruvate: step 3/4.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
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DR EMBL; BX548174; CAE19233.1; -; Genomic_DNA.
DR RefSeq; NP_892892.1; NC_005072.1.
DR ProteinModelPortal; Q7V1T1; -.
DR STRING; 59919.PMM0774; -.
DR PRIDE; Q7V1T1; -.
DR EnsemblBacteria; CAE19233; CAE19233; PMM0774.
DR GeneID; 1725819; -.
DR KEGG; pmm:PMM0774; -.
DR PATRIC; 23032404; VBIProMar68066_0870.
DR eggNOG; COG0129; -.
DR HOGENOM; HOG000173155; -.
DR KO; K01687; -.
DR OMA; NMPGAMI; -.
DR ProtClustDB; PRK00911; -.
DR BioCyc; PMAR59919:GJMQ-796-MONOMER; -.
DR UniPathway; UPA00047; UER00057.
DR UniPathway; UPA00049; UER00061.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:HAMAP.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:HAMAP.
DR HAMAP; MF_00012; IlvD; 1; -.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR004404; DihydroxyA_deHydtase.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR PANTHER; PTHR21000; PTHR21000; 1.
DR Pfam; PF00920; ILVD_EDD; 1.
DR SUPFAM; SSF52016; Aconitase/3IPM_dehydase_swvl; 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 4Fe-4S; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Complete proteome; Iron;
KW Iron-sulfur; Lyase; Metal-binding.
FT CHAIN 1 559 Dihydroxy-acid dehydratase.
FT /FTId=PRO_0000103491.
FT METAL 122 122 Iron-sulfur (4Fe-4S) (Potential).
FT METAL 194 194 Iron-sulfur (4Fe-4S) (Potential).
SQ SEQUENCE 559 AA; 59461 MW; 1C753D5A38B45F1B CRC64;
MNKLRSSAIT QGVQRSPNRS MLRAVGFSDE DFTKPIIGVA NGFSTITPCN MGLNKLALKA
EESIREAGGM PQMFGTITVS DGISMGTEGM KYSLVSREVI ADSIETACNA QSMDGVLAIG
GCDKNMPGAM IAIARMNIPS IFIYGGTIKP GKLNGEDLTV VSAFEAVGQL TSGKINEKRL
IEVEKNCIPG AGSCGGMFTA NTMSAVIEVL GLSLPYSSTM AAEDYEKEVS AEKSAEILVD
AIRKDIRPLT LMTKESFENA ITVIMAIGGS TNAVLHILAI ANTAGIDINI DDFERIRQKV
PVICDLKPSG KYVTVDLHKA GGIPQVMKIL LNTGLIHGNC RNIEGKTVVE SLKDIPVKPP
ENQDVIRDID NPLYKKGHLA ILKGNLASEG CVAKISGIKN PVLKGPARIF ESEEDCLKSI
LNNDIKAGNV VVIRNEGPVG GPGMREMLAP TSAIVGQGLG EKVALITDGR FSGGTYGLVV
GHIAPEAAVG GNIALIKEGD LITVDATNQL IEVELSDEEL EMRRINWEKP SKKYKKGVLS
KYSRIVSTSS LGAVTDLEE
//
