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Database: UniProt
Entry: A0A244EIN5_9BURK
LinkDB: A0A244EIN5_9BURK
Original site: A0A244EIN5_9BURK 
ID   A0A244EIN5_9BURK        Unreviewed;       581 AA.
AC   A0A244EIN5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:OUM04323.1};
GN   ORFNames=A8M77_01035 {ECO:0000313|EMBL:OUM04323.1};
OS   Variovorax sp. JS1663.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1851577 {ECO:0000313|EMBL:OUM04323.1, ECO:0000313|Proteomes:UP000195166};
RN   [1] {ECO:0000313|EMBL:OUM04323.1, ECO:0000313|Proteomes:UP000195166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS1663 {ECO:0000313|EMBL:OUM04323.1};
RX   PubMed=28526789;
RA   Mahan K.M., Zheng H., Fida T.T., Parry R.J., Graham D.E., Spain J.C.;
RT   "A novel, iron-dependent enzyme that catalyzes the initial step in the
RT   biodegradation of N-nitroglycine by Variovorax sp. strain JS1663.";
RL   Appl. Environ. Microbiol. 83:0-0(2017).
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:OUM04323.1}.
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DR   EMBL; LYMK01000001; OUM04323.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A244EIN5; -.
DR   OrthoDB; 9807077at2; -.
DR   Proteomes; UP000195166; 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: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.
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:UP000195166}.
SQ   SEQUENCE   581 AA;  61896 MW;  806E001B685C27E7 CRC64;
     MPDAPKKLRS AQWFGPADKN GFMYRSWMKN QGIPDHEFDG RPIVGICNTW SELTPCNAHF
     RKLAEHVKRG ISEAGGFPVE FPVFSNGESN LRPTAMLTRN LASMDVEEAI RGNPIDAVVL
     LAGCDKTTPA LLMGAASCDV PAIVVSGGPM LNGKLEGRDI GSGTAVWQLH ESLKAGEIDL
     HQFLAAEGGM SRSAGTCNTM GTASTMACMA EALGVALPHN AAIPAVDARR YVLAQMSGAR
     VVAMAKEGLT LSKILTREAF ENAIRVNAAI GGSTNAVIHL KAIAGRIGVD LALEDWTRIG
     RGTPTLVDLL PSGRFLMEEF YYAGGLPAVL RRLGEAGLLP HPDAPTVNGR SLWDNVRDAP
     SYNDEVIRPL DKPLLDDGGI CILRGNLAPR GAVLKPSAAT PELLKHRGRA VVFEDFDDYK
     RRIGDESLEV DASSVLVMKN CGPRGYPGMA EVGNMGLPPK LLRQGIKDMV RISDARMSGT
     AYGTVVLHVA PEAAAGGPLA AVRDGDWIEL DCEAGRLHLD VGDEELAARL AARASAQPAA
     PPAARGGYAR LYVDHVLQAD EGCDFDFLVG CRGAEVPRHS H
//
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