ID A0A0L6T592_9BURK Unreviewed; 605 AA.
AC A0A0L6T592;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KNZ31314.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:KNZ31314.1};
GN ORFNames=AD742_18875 {ECO:0000313|EMBL:KNZ31314.1};
OS Methylibium sp. NZG.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=1686064 {ECO:0000313|EMBL:KNZ31314.1, ECO:0000313|Proteomes:UP000053102};
RN [1] {ECO:0000313|Proteomes:UP000053102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bi G.;
RT "Draft Genome Sequences of the MTBE Degrading Bacterium Methylibium sp.
RT NZG.";
RL Submitted (JUL-2015) 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:KNZ31314.1}.
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DR EMBL; LGRD01000032; KNZ31314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6T592; -.
DR STRING; 1686064.AD742_18875; -.
DR PATRIC; fig|1686064.3.peg.3668; -.
DR Proteomes; UP000053102; Unassembled WGS sequence.
DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:KNZ31314.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053102}.
SQ SEQUENCE 605 AA; 65971 MW; DF16ECA6B928AC76 CRC64;
MNSKKPGAKK RIKPSQLRSR AWFDNPANAD MTALYLERTM NFGLSMEELQ SGRPMIGIAQ
SGSDIAPCNR HHLVLAQRMR EGIRDAGGVA FEFPLHPIQE TCKRPTAALD RNLQYLALVE
VLYGYPLDGV ILTTGCDKTT PAQLMAAATV DIPAIAINSG PMLNGWHDGE RTGSGTIVWK
ARQMMAKGDI DYPQFLKLVA SSAPSTGHCN TMGTASTMNA LTEAMGMCLP GTAAIPAPYR
DRQEAAYLTG KRIVEMVWEN LKPSDIMTRE AFENVIVVNS AIGGSTNAPV HINAIARHIG
VKLDNDDWEK IGYELPLLVN MQPAGEYLGE EYYRAGGLPA VVAELVKKGK IKPSPTVNGK
TLAENCEGQF STDRRVILPY DKPMQKKAGF LNLKGNLFDS AIMKTSVITK EFRERYLENP
ADPMAFEGKA VVFDGPEDYH HRIDDPKTKI DAHTVLFIRG VGPVGYPGAA EVVNMRPPNY
LIKQGVTALP CIGDGRQSGT SGSPSILNAS PEAATGGGLA LLKTGDRVRI DLKKRTANIL
ISDAELQKRR EALEAAGGYK YPPSQTPWQE IQRGIVDELS HGMVLKPAVK YQKIHATFGV
PRDNH
//