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Database: UniProt
Entry: A0A1H7DM81_9ACTN
LinkDB: A0A1H7DM81_9ACTN
Original site: A0A1H7DM81_9ACTN 
ID   A0A1H7DM81_9ACTN        Unreviewed;       575 AA.
AC   A0A1H7DM81;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:SEK02883.1};
GN   ORFNames=SAMN05443287_11547 {ECO:0000313|EMBL:SEK02883.1};
OS   Micromonospora phaseoli.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1144548 {ECO:0000313|EMBL:SEK02883.1, ECO:0000313|Proteomes:UP000198707};
RN   [1] {ECO:0000313|Proteomes:UP000198707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.7038 {ECO:0000313|Proteomes:UP000198707};
RA   Varghese N., Submissions S.;
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; FNYV01000015; SEK02883.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7DM81; -.
DR   STRING; 1144548.SAMN05443287_11547; -.
DR   OrthoDB; 9807077at2; -.
DR   Proteomes; UP000198707; 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}.
SQ   SEQUENCE   575 AA;  61237 MW;  0C99F9F20956852E CRC64;
     MSMTNRPLRS GQWFGADGRN GFIHRSWMRN QGFADDVFDG RPVIGIATTW SELTPCNAHL
     RELAESVKRG IWESGGLPLE FPAMSLGEPL MRPTTMLYRN LLAMEAEELI RANPLDGVVL
     LSGCDKTTPG LLMGAASVDL PTLLITGGPM LNGKFRGQDI GSGTSVWRFT EELRAGRMTV
     ADCAEAEVCM SRSRGHCMTM GTASTMACVT EALGVQLPGA AAVPAVDSRR YALAHAAGRR
     IVAMVEQDQR LSTVLTRPAF ENAIRVNAAI GGSTNAVVHL LAIAGRIGVP LSLEDFGTLT
     TDVPMLVNLM PSGTYLMEDF AYAGGVPAVM KEIAPLLHLD QITVSGKSVA DNISGVQCWN
     RQVIGTLTEP FQPAGSGTVV LRGSLAPSGA VLKVSAASAH LLTHTGPALV FDRIEEYAVA
     ADDPDLDVTP DTVIVVRNAG PRGYPGFPEV GNVPMPRRLL ANGVTDMVRI SDARMSGTGY
     GTCVLHVAPE ASVGGPLALV RTGDLVHLDV PTRRLDLLVD EVELAHRRAA WQPPPPAADR
     GWVRLYSEHV QQADRGADLD FLVGGSGSEV PRHSH
//
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