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Database: UniProt
Entry: A0A1H0ILE0_9BRAD
LinkDB: A0A1H0ILE0_9BRAD
Original site: A0A1H0ILE0_9BRAD 
ID   A0A1H0ILE0_9BRAD        Unreviewed;       578 AA.
AC   A0A1H0ILE0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Dihydroxyacid dehydratase {ECO:0000313|EMBL:SDO32299.1};
GN   ORFNames=SAMN05444050_3851 {ECO:0000313|EMBL:SDO32299.1};
OS   Afipia sp. GAS231.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=1882747 {ECO:0000313|EMBL:SDO32299.1, ECO:0000313|Proteomes:UP000198617};
RN   [1] {ECO:0000313|EMBL:SDO32299.1, ECO:0000313|Proteomes:UP000198617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAS231 {ECO:0000313|EMBL:SDO32299.1,
RC   ECO:0000313|Proteomes:UP000198617};
RA   de Groot N.N.;
RL   Submitted (OCT-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; LT629703; SDO32299.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0ILE0; -.
DR   STRING; 1882747.SAMN05444050_3851; -.
DR   OrthoDB; 7793094at2; -.
DR   Proteomes; UP000198617; Chromosome i.
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:SF2; DIHYDROXY-ACID DEHYDRATASE; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198617}.
SQ   SEQUENCE   578 AA;  63241 MW;  6DFA1BB019BB258B CRC64;
     MTARKNPADL RSARWFAPDD LRAFGHRSRA MQMGYAPEEW KDRPVIAILN TWSDAQPCHM
     HFKSRVEDVK RGILMAGGFP MELPALSLSE SFLKPTTMLY RNMLAMDAEE LLRGHPVDGV
     VLMGGCDKTT PGLLLGATSM GLPAIYLPAG PMLRGNWKGK TLGSGSDAWK FWDERRAGKI
     SDKDWVDVEA GIARSYGTCM TMGTASTMTA IAESIGMTLP GASSIPAADA GHIRMASESG
     RRIVEMVWED LTPNKIQTRK AFENAITVAM AMGCSTNAII HLIAQARRAG QDIGLDDFEI
     ASRKVPVIAN VRPSGDKYLM EDFFYAGGLP GLMSRIKEHL HLDVMTVTGQ TLGDNIARAE
     VYNDDVIRTV KDPIYAEGAL AVLRGNLAPD GCVIKPSACE PRFLKHTGPA LVFDDYPSMK
     KAVDDPNLDV TADHVMILRN AGPQGGPGMP EWGMLPIPTK LVKQGVRDMV RLSDARMSGT
     SYGACILHVA PEAYIGGPLA LVRNGDRITL DVNARTINLE VSEAELAKRR AEWKPPERRY
     ERGYGWMFTK HIKQANEGCD FDFLETGFGA PVGEPSIY
//
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