ID   A8TVN5_9PROT            Unreviewed;       574 AA.
AC   A8TVN5;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:EDP63362.1};
GN   ORFNames=BAL199_20305 {ECO:0000313|EMBL:EDP63362.1};
OS   alpha proteobacterium BAL199.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP63362.1, ECO:0000313|Proteomes:UP000003417};
RN   [1] {ECO:0000313|EMBL:EDP63362.1, ECO:0000313|Proteomes:UP000003417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL199 {ECO:0000313|EMBL:EDP63362.1,
RC   ECO:0000313|Proteomes:UP000003417};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC       {ECO:0000256|ARBA:ARBA00006486}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDP63362.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ABHC01000014; EDP63362.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8TVN5; -.
DR   STRING; 331869.BAL199_20305; -.
DR   eggNOG; COG0129; Bacteria.
DR   OrthoDB; 9807077at2; -.
DR   Proteomes; UP000003417; 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   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR   InterPro; IPR037237; IlvD/EDD_N.
DR   PANTHER; PTHR43183:SF2; DIHYDROXY-ACID DEHYDRATASE; 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.
DR   PROSITE; PS00886; ILVD_EDD_1; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003417}.
SQ   SEQUENCE   574 AA;  63008 MW;  C71756618B993ADD CRC64;
     MVRKRYEDLR SYRWYGADDL RSFGHRSRTL QMGYDRADWT GKPVIAVINT WSEINPCHTH
     FKARAEEVKR GIWQAGGFPV ELPAISLSEP FQKPTTMMYR NLLALEVEEL MRSYPCDGAV
     LMGGCDKTTP ALLMGAASMN LPSIFVPAGP MLRGNWRGKS LGSGSDTWKY WAELQVGNIT
     RKDWEEIEDG IARTPGTCMT MGTAATMMSS VEGLGMSLPG SSAIPAADSN HSRMASQSGR
     RIVEMVWEDQ KPSDVMTEKA FENAITTVMA LGGSTNAVIH LMAMAGRLGV PIDLDRFDAL
     SRKTPWLADI RPSGRFLMED FYYAGGLPAM LSELKEQLHL DAVTVSGKTL GEDIERADIH
     NEEVIRRSAS PLSKEGGLVV LRGNLAPDGA IIKQTACDPK LLKHRGPAVV FADYNDMQAR
     LNDPDLDVTA DSVIVLKHAG PQGGPGMPEW GMLPIPKKIL QLGVRDMVRI SDARMSGTSY
     GTCVLHVAPE SWVGGPLAFV QDGDMIELDV HGRRLHLDVS DAELDARRAA WIPPARKFER
     GFGAIYAEHI TQADKGCDFD VLMGTKATPE PEIH
//