ID A0A076MR01_AMYME Unreviewed; 574 AA.
AC A0A076MR01;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:AIJ21371.1};
GN Name=ilvD {ECO:0000313|EMBL:AIJ21371.1};
GN ORFNames=AMETH_1279 {ECO:0000313|EMBL:AIJ21371.1};
OS Amycolatopsis methanolica 239.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ21371.1, ECO:0000313|Proteomes:UP000062973};
RN [1] {ECO:0000313|EMBL:AIJ21371.1, ECO:0000313|Proteomes:UP000062973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=239 {ECO:0000313|EMBL:AIJ21371.1,
RC ECO:0000313|Proteomes:UP000062973};
RA Tang B.;
RT "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL Submitted (JUL-2014) 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; CP009110; AIJ21371.1; -; Genomic_DNA.
DR RefSeq; WP_017987232.1; NZ_CP009110.1.
DR AlphaFoldDB; A0A076MR01; -.
DR STRING; 1068978.AMETH_1279; -.
DR KEGG; amq:AMETH_1279; -.
DR PATRIC; fig|1068978.7.peg.1348; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_3_1_11; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000062973; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000062973}.
SQ SEQUENCE 574 AA; 61099 MW; 0561CE3CA3774FFB CRC64;
MTGQRRSAAW FGATGRAGMI YRSWMRNQGF GAEVFDGRPV IGIATSASEL APCNAHLTRV
AEAVKRGVWQ AGGFPLEFPT MATGETLMRP TAMLYRNLMA MEVEELIRAN PLDGVVLLSG
CDKTTPAMLM AAASVDLPAV MVTGGPMLNG KYRGADVGSG THVWKFEEEL KAGRMTQEEC
FFAEGCMARS NGHCMTMGTA STMACMAEAL GMQLPGSATW PAVDARRFEI GQSAGQRIVE
MAEEDLRPSH ILTREAFENA IRVNAAIGGS TNAIIHLLAI AGRAEVDLTL DDFDTLIRDV
PTLVNLMPSG KYLMEDFCYA GGLPVVMRQL AEAGLLHTGS VSVTGKPVGE NVAAAENFNT
DVITTVEEPF QPAGNGTAVL RGNLCPGGAV IKQSAASPHL LKHQGRALVF DTVEDYHAVA
DDPDLDVDET SILVIRGAGP KGYPGMPEVS NVALPAKLLK AGVTDMIRIC DGRMSGTGYG
TVVLHVTPES AAGGPLALVR TGDLITLDVA ARTLNVEVSD EELAARRASW RAPGSPYTSG
YTWLYTEHVL QADQGADFDF LRGSRGHSVP RDSH
//
