ID M4S292_9SPHN Unreviewed; 598 AA.
AC M4S292;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:AGH49023.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:AGH49023.1};
GN ORFNames=G432_06490 {ECO:0000313|EMBL:AGH49023.1};
OS Sphingomonas sp. MM-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=745310 {ECO:0000313|EMBL:AGH49023.1, ECO:0000313|Proteomes:UP000011816};
RN [1] {ECO:0000313|EMBL:AGH49023.1, ECO:0000313|Proteomes:UP000011816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM-1 {ECO:0000313|EMBL:AGH49023.1};
RX PubMed=23682148;
RA Tabata M., Ohtsubo Y., Ohhata S., Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of the gamma-Hexachlorocyclohexane-Degrading
RT Bacterium Sphingomonas sp. Strain MM-1.";
RL Genome Announc. 1:E00247-13(2013).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; CP004036; AGH49023.1; -; Genomic_DNA.
DR RefSeq; WP_015458036.1; NC_020561.1.
DR AlphaFoldDB; M4S292; -.
DR STRING; 745310.G432_06490; -.
DR KEGG; sphm:G432_06490; -.
DR PATRIC; fig|745310.14.peg.1346; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_3_1_5; -.
DR Proteomes; UP000011816; Chromosome.
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:AGH49023.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011816}.
SQ SEQUENCE 598 AA; 64131 MW; 39A4D3FD5B4999F9 CRC64;
MTDTAPPKLR SRAWFDNPDN IDMTALYLER YLNFGLSLEE LRSGKPIIGI AQTGSDLSPC
NRHHLVLAER IREGIREAGG IALEFPVHPI QETGKRPTAG LDRNLAYLGL VEAIYGYPID
GVVLTTGCDK TTPACLMAAA TVNIPAIALS VGPMLNGWHK GERTGSGTIV WKARQMLAAG
QIDNAGFIKL VASSAPSTGY CNTMGTATTM NSLAEALGMM LPGSAAIPAP YRDRQEVAYL
TGKRIVEMVA EDLKPSDILT LDAFHNAIVV NSAIGGSTNA PIHLAAIARH IGVDLPLKDW
ETEGHKVPLL VNLQPAGEYL GEDYYRAGGV PAVVAQLMGQ GLIREAAMTV NGRTIGDNCR
DATIEDERVI RPFDQPLKEE AGFLVLTGNL FDAAIMKTSV ISPEFRDRYL SNPDDPDAFE
GPAVVFDGPE DYHHRIDDPS LGITPQTLLF MRGAGPIGYP GAAEVVNMRP PAYLITEGVS
ALPCIGDGRQ SGTSGSPSIL NASPEAAANG GLALLRTGDR VRLDLRRGRV DVLISDAELA
DRRKALEAAG GYAYPASQTP WQEIQRKIVG QMDTGAILEG AEKYQRIAQT RGLPRDNH
//
