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Database: UniProt
Entry: J0CM37_RHILT
LinkDB: J0CM37_RHILT
Original site: J0CM37_RHILT 
ID   J0CM37_RHILT            Unreviewed;       579 AA.
AC   J0CM37;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Dihydroxyacid dehydratase/phosphogluconate dehydratase {ECO:0000313|EMBL:EJC80635.1};
GN   ORFNames=Rleg4DRAFT_2269 {ECO:0000313|EMBL:EJC80635.1};
OS   Rhizobium leguminosarum bv. trifolii WSM2297.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=754762 {ECO:0000313|EMBL:EJC80635.1, ECO:0000313|Proteomes:UP000005732};
RN   [1] {ECO:0000313|EMBL:EJC80635.1, ECO:0000313|Proteomes:UP000005732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM2297 {ECO:0000313|EMBL:EJC80635.1,
RC   ECO:0000313|Proteomes:UP000005732};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R.,
RA   O'Hara G., Rui T., Howieson J., Reeve W., Woyke T.;
RT   "Improved High-Quality Draft Sequence of Rhizobium leguminosarum bv.
RT   trifolii WSM2297.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC       {ECO:0000256|ARBA:ARBA00006486}.
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DR   EMBL; JH719395; EJC80635.1; -; Genomic_DNA.
DR   AlphaFoldDB; J0CM37; -.
DR   HOGENOM; CLU_014271_3_1_5; -.
DR   OrthoDB; 7793094at2; -.
DR   Proteomes; UP000005732; Unassembled WGS sequence.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR   InterPro; IPR042096; Dihydro-acid_dehy_C.
DR   InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR   InterPro; IPR037237; IlvD/EDD_N.
DR   PANTHER; PTHR43183:SF1; HYPOTHETICAL DIHYDROXY-ACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR43183; HYPOTHETICAL DIHYDROXYACID DEHYDRATASE (EUROFUNG)-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.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ   SEQUENCE   579 AA;  62598 MW;  F032A73B02D48D4F CRC64;
     MKKKAEWPRR LRSQEWYGGT SRDVIYHRGW LKNQGYPHDL FDGRPVIGIL NTWSDMTPCN
     GHLRELAEKV KAGVWEAGGF PLEVPVFSAS ENTFRPTAMM YRNLAALAVE EAIRGQPMDG
     CVLLVGCDKT TPSLLMGAAS CDLPSIVVTG GPMLNGYFRG ERVGSGTHLW KFSEMVKAGE
     MTQAEFLEAE ASMSRSSGTC NTMGTASTMA SMAEALGMAL SGNAAIPGVD SRRKVMAQLT
     GRRIVQMVKD DLKPSEIMTK EAFENAIRTN AAIGGSTNAV IHLLAIAGRV GIDLSLDDWD
     RCGRDVPTIV NLMPSGKYLM EEFFYAGGLP VVLKRLGEAG LLHKDALTVS GETVWNEVKD
     VVNWNEDVIL PAEKALTSSG GIVVLRGNLA PKGAVLKPSA ASPHLLVHKG RAVVFEDIDD
     YKAKINDDNL DIDETCIMVM KNCGPKGYPG MAEVGNMGLP PKVLKKGILD MVRISDARMS
     GTAYGTVVLH TSPEAAVGGP LAVVKNGDMI ELDVPNRRLH LDISDEELAR RLAEWQPNHD
     LPTSGYAFLH QQHVEGADTG ADLDFLKGCR GNAVGKDSH
//
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