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Database: UniProt
Entry: A0A158IP65_9BURK
LinkDB: A0A158IP65_9BURK
Original site: A0A158IP65_9BURK 
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
//
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