ID A0A158IP65_9BURK Unreviewed; 594 AA.
AC A0A158IP65;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:SAL57999.1};
GN ORFNames=AWB65_05122 {ECO:0000313|EMBL:SAL57999.1};
OS Caballeronia humi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=326474 {ECO:0000313|EMBL:SAL57999.1, ECO:0000313|Proteomes:UP000054977};
RN [1] {ECO:0000313|EMBL:SAL57999.1, ECO:0000313|Proteomes:UP000054977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22934 {ECO:0000313|EMBL:SAL57999.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; FCNW02000038; SAL57999.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158IP65; -.
DR STRING; 326474.AWB65_05122; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000054977; 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}.
FT REGION 483..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 594 AA; 63758 MW; C2D0DA21BDEA4BCA CRC64;
MSQPHVRRLR SQEWFDDPSH ADMTALYVER FMNYGLTRDE LQSGRPIIGI AQTGSDLAPC
NRHHIELAAR TKAGIRDAGG IPMEFPVHPL AEQSRRPTAA LDRNLAYLGL VEILHGFPLD
GVVLTTGCDK TTPACLMAAA TVDLPAIVLS GGPMLDGWHQ GKRVGSGTVI WHARNLLATG
EIDYEGFMEL TTASSPSIGH CNTMGTALSM NSLAEALGMS LPGCASIPAA YRERGQMAYV
TGKRIVDLVR EDVRPSHILT KEAFENAIVV ASALGASTNC PPHLIAIARH IGVELSLDDW
QRVGEQVPLI VNCMPAGEYL GESFHRAGGV PAVLRELVQA GLVHRACKTV SGSTIGEIAA
AAPAPDREVI KTADEPLKHG AGFIVLSGNF FDSAIMKMSV VGDAFRQTYL SEPGAENTFE
ARAIVFDGPE DYHARINDPS LEIDQHCILV IRGAGTVGYP GSAEVVNMAP PASLVKQGIT
SLPTLGDGRQ SGTSASPSIL NMSPEAAVGG GLSLLRTNDR IRVDLSARSV NVLVEDEELE
RRRQTVTFDI PRSQTPWQEL YRQTVGQLST GGCLEPATLY LKVIAERGNP RHSH
//