ID A0A101U7M3_9ACTN Unreviewed; 570 AA.
AC A0A101U7M3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KUO05558.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:KUO05558.1};
GN ORFNames=AQJ67_05255 {ECO:0000313|EMBL:KUO05558.1};
OS Streptomyces caeruleatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=661399 {ECO:0000313|EMBL:KUO05558.1, ECO:0000313|Proteomes:UP000053429};
RN [1] {ECO:0000313|EMBL:KUO05558.1, ECO:0000313|Proteomes:UP000053429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24802 {ECO:0000313|EMBL:KUO05558.1,
RC ECO:0000313|Proteomes:UP000053429};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces caeruleatus NRRL B-24802, type
RT strain for the species Streptomyces caeruleatus.";
RL Submitted (OCT-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:KUO05558.1}.
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DR EMBL; LMWY01000004; KUO05558.1; -; Genomic_DNA.
DR RefSeq; WP_062716848.1; NZ_KQ948925.1.
DR AlphaFoldDB; A0A101U7M3; -.
DR STRING; 661399.AQJ67_05255; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000053429; 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 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, ECO:0000313|EMBL:KUO05558.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053429}.
SQ SEQUENCE 570 AA; 60276 MW; A1EA7B380A5F6315 CRC64;
MKLRSAQWYA GQDRNAYIHR AWMRRGVPDD AFTGRPQIAI ANTASDLTPC NAHLNEVAAS
VRNGVYEAGG IPLDLPVVSL GETNVRPTAM LWRNMAAMAT EEMLRANPVD GVVLLGGCDK
TIPSLLMAAA SVDLPAVVVP GGPMLNGSFR GKSLGCGTDV WRLSEEVRGG TLSQADFTSS
ESAMIRSRGH CNTMGTASTM ALVAEALGTV VPGVAGTPAP DSRLLQAAHE TGRLAVEMVG
ADRRPGTFLT KASFHNAIVA LAAVGGSTNA VVHLLAIAGR LGVDLCLDHF DRIGSRVPVL
VDLQPAGRFL MEDFHRAGGL LAVLHEVRDL LDPDALTVTG RPLVEHLDGA AVWDADVIRP
REQPLVAEGG IAVLRGNLAP DGALIKPAAA SPHLLEHRGR AAVFDSIEDF HARIDDPDLE
VDADSVLVLR GCGPKGYPGM PEVSNMPLPK KLLEQGVRDM VRICDGRMSG TAYGTVVLHV
APEAAAGGPL ALVRTGDIVS LDVKARRIDV DVPADELARR TPNKSTLDGF ANPKRGWERL
YVDHVQQAHT GADLDFLVGS SGSGVSRESH
//
