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Database: UniProt
Entry: A0A1Q4D5C0_9PSEU
LinkDB: A0A1Q4D5C0_9PSEU
Original site: A0A1Q4D5C0_9PSEU 
ID   A0A1Q4D5C0_9PSEU        Unreviewed;       565 AA.
AC   A0A1Q4D5C0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:OJY39375.1};
GN   ORFNames=BGP03_06120 {ECO:0000313|EMBL:OJY39375.1};
OS   Pseudonocardia sp. 73-21.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1895809 {ECO:0000313|EMBL:OJY39375.1, ECO:0000313|Proteomes:UP000186163};
RN   [1] {ECO:0000313|EMBL:OJY39375.1, ECO:0000313|Proteomes:UP000186163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-21 {ECO:0000313|EMBL:OJY39375.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJY39375.1}.
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DR   EMBL; MKVV01000096; OJY39375.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q4D5C0; -.
DR   STRING; 1895809.BGP03_06120; -.
DR   Proteomes; UP000186163; 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   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; 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.
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}.
SQ   SEQUENCE   565 AA;  59863 MW;  53F197F02881941C CRC64;
     MELRSTHWYA GEDRNAYIHR AWMRRGLPGD AFTGRPQIAI ANTASDLTPC NAHLTEVAAS
     VRNGVYEAGG IPLELPVVSL GETNVRPTAM LWRNMAAMAT EEMLRANPID AVVLLGGCDK
     TIPSLLMAAA SVDIPAVVVP GGPMLTGTFR GTPLGCGTDV WRLSEEVRAG TLTQEAFSRS
     ESSMIRSRGH CNTMGTASTM GLVAEALGTV IPGVAGTPAP DSRLLEAAHG TGRLIVEMLA
     ADRRPSTFLT KASFHNAIVA LAAIGGSTNA VVHLLAIAGR LGIELGVDDF DRIGSRVPVL
     VDLQPAGRFL MEDLHRAGGL LAVLREVRDL LDPTALTVTG KPLVDHLDDT PIFDTEVIRP
     RTAPLVAEGG IAVLRGNLAP DGALIKPAAA SPHLLQHRGR AMVFDSIEDF HARIDDPDLD
     VDADSVLVLR GCGPKGYPGM PEVSNMPLPR KLLEQGVRDM VRVCDGRMSG TAYGTVVLHV
     APEAAAGGPL ARVRTGDVIV LDVAARRIDV ETDDLDARTP STAGFANPRR GWERLYVDHV
     QQADTGADLD FLVGSSGSEV GRESH
//
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