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Database: UniProt
Entry: A0A1G6V1W8_9ACTN
LinkDB: A0A1G6V1W8_9ACTN
Original site: A0A1G6V1W8_9ACTN 
ID   A0A1G6V1W8_9ACTN        Unreviewed;       570 AA.
AC   A0A1G6V1W8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:SDD46946.1};
GN   ORFNames=SAMN04489747_1009 {ECO:0000313|EMBL:SDD46946.1};
OS   Auraticoccus monumenti.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Auraticoccus.
OX   NCBI_TaxID=675864 {ECO:0000313|EMBL:SDD46946.1, ECO:0000313|Proteomes:UP000198546};
RN   [1] {ECO:0000313|EMBL:SDD46946.1, ECO:0000313|Proteomes:UP000198546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MON 2.2 {ECO:0000313|EMBL:SDD46946.1,
RC   ECO:0000313|Proteomes:UP000198546};
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; LT629688; SDD46946.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6V1W8; -.
DR   STRING; 675864.SAMN04489747_1009; -.
DR   OrthoDB; 9807077at2; -.
DR   Proteomes; UP000198546; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198546}.
SQ   SEQUENCE   570 AA;  60113 MW;  A10A0F60A9540720 CRC64;
     MGLRSAEWYA GDDRNAYIHR AWMRRGLPDD AFTGRPHVAI ATTASDLTPC NSHLGEVARS
     VANGVYEAGG IPLELPVVSL GETLVRPTAM LWRNLAAMAT EELLRANPVD AVVLLGGCDK
     TIPSLLMGAA SVDLPAVVVP GGPMLTGTFR GVPLGCGTDV WRLSEEVRGG TLSEQDFLRS
     ESAMIRSRGH CNTMGTASTM SLLAEALGMV VPGLAGTPAP DSRLLEGAHG TGRLAVGLVA
     ADRRPSTVLT RASFHNAIVA LAAIGGSTNA VVHLLALAGR LGVELTLDDF DRIGADVPLL
     VNLQPAGRHL MEDLHRAGGF LAVLREVRDL LDPDALTVTG RPLVEHLDEA RVWDADVISP
     RGEPLLPAAG IAVLRGSLAP DGAIVKPAAA SAHLLRHRGR ALVFDSIEDF HARIDDPDLD
     VDADSVLVLR GCGPRGYPGM PEVANMPLPT KLLEQGVRDM VRICDGRMSG TAYGTVVLHV
     APEAAAGGPL GLVRTGDWIV LDVPARRLDL DVDPAELAAR TPDEATVAGY ARPTRGWERL
     YVDHVQQADR GADLDFLVGS SGSAVSRESH
//
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