ID A0A0Q6L2L8_9SPHN Unreviewed; 598 AA.
AC A0A0Q6L2L8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KQU62084.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:KQU62084.1};
GN ORFNames=ASG67_02825 {ECO:0000313|EMBL:KQU62084.1};
OS Sphingomonas sp. Leaf339.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736343 {ECO:0000313|EMBL:KQU62084.1, ECO:0000313|Proteomes:UP000051371};
RN [1] {ECO:0000313|EMBL:KQU62084.1, ECO:0000313|Proteomes:UP000051371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf339 {ECO:0000313|EMBL:KQU62084.1,
RC ECO:0000313|Proteomes:UP000051371};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQU62084.1, ECO:0000313|Proteomes:UP000051371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf339 {ECO:0000313|EMBL:KQU62084.1,
RC ECO:0000313|Proteomes:UP000051371};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQU62084.1}.
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DR EMBL; LMRS01000001; KQU62084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q6L2L8; -.
DR STRING; 1736343.ASG67_02825; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000051371; 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:KQU62084.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000051371}.
SQ SEQUENCE 598 AA; 64052 MW; 22D87A4A05C47774 CRC64;
MTMTDRPKLR SRAWFDNPDN IDMTALYLER YLNFGLSLEE LQSGKPIIGI AQTGSDLSPC
NRHHLVLAER VREGVRDMGG IVLEFPVHPI QETGKRPTAG LDRNLAYLAL VEVLYGYPLD
GVVLTIGCDK TTPACLMAAA TVNIPAIALS VGPMLNGWHK GERTGSGTIV WKARQLLAAG
EIDDAEFIRL VSSSAPSTGY CNTMGTATTM NSLCEALGMS LPGSAAIPAP YRDRQEVAWR
TGKRIVEMVA EDLKPSDILT RPAFHNAIKV NSAIGGSTNA PIHLAAIARH IGVDLPLKDW
ETEGHKVPLL VNLQPAGEYL GEDYYRAGGV PAVVNQLMGQ GLIAEDALTV NGRTMGDNCR
GVAIEDEKVI RPFAEPLKEE AGFIVLSGNL FDAAVMKTSV IGPEFRERYL SNPDDPEAFE
GPAVVFDGPE DYHHRIDDPS VGITPETLLF MRGAGPIGYP GAAEVVNMRP PAYLITEGVH
ALPCIGDGRQ SGTSGSPSIL NASPEAAAGG MLALLRTGDR VRVDLGKGTV DALVPMEELA
ARRAALQAAG GYAYPASQTP WQEISRGHVG QMNTGAIIEG AEKYQRIAQT KGLPRDNH
//
