ID W2EK41_9ACTN Unreviewed; 564 AA.
AC W2EK41;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:ETK32073.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:ETK32073.1};
GN ORFNames=MPTA5024_31645 {ECO:0000313|EMBL:ETK32073.1};
OS Microbispora sp. ATCC PTA-5024.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK32073.1, ECO:0000313|Proteomes:UP000018869};
RN [1] {ECO:0000313|EMBL:ETK32073.1, ECO:0000313|Proteomes:UP000018869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK32073.1,
RC ECO:0000313|Proteomes:UP000018869};
RX PubMed=24459268;
RA Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A.,
RA Stegmann E., Weber T.;
RT "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024,
RT Producing the Lantibiotic NAI-107.";
RL Genome Announc. 2:e01198-13(2014).
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:ETK32073.1}.
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DR EMBL; AWEV01000255; ETK32073.1; -; Genomic_DNA.
DR RefSeq; WP_036330679.1; NZ_KI866525.1.
DR AlphaFoldDB; W2EK41; -.
DR STRING; 316330.MPTA5024_31645; -.
DR PATRIC; fig|316330.3.peg.6101; -.
DR HOGENOM; CLU_014271_3_1_11; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000018869; 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 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:SF2; DIHYDROXY-ACID DEHYDRATASE; 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, ECO:0000313|EMBL:ETK32073.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018869}.
SQ SEQUENCE 564 AA; 61198 MW; D1712D609868A8B4 CRC64;
MRPEELRSHR WYGTDGLRSF SHRARTRQLG LSAEEHLGKP VIGILNTWSE LNPCHIHLRE
RAEDVRRGVW QAGGYPVELP VMAVGETFQK PTAMLYRNLL AMETEEVLRS YPVDAAVLMG
GCDKTTPALL MGAISADLPS IFVPCGPMLP GDWRGRRLGS GSDMWKYWAD RRAGLVTDEE
WREIEDGIAR SPGHCMTMGT ASTMTSVAEV LGMTMPGAAS IPAVLSAHNR MAAESGRTAV
RLAWEDVRPS RLLGERAYRD ALTAVLALGG STNAVIHLIA MARRSGVALT LDDFDEASRR
VPVLADIRPT GAFLMEDFHR AGGVPALLHR VADLLHLDRP TVAGHGVATR EPYDDTVIRR
RDDPLSPEGG LAVLRGNLAP DGAVIKHAAA EPRLLRHTGP AIVFDGHRDL LARIDDVPAT
PGSVLVLRGA GPKGGPGMPE HGMLPIPGRL LKQGVRDMVR ISDARMSGTS YGACVLHVAP
ESHVGGPLAL VRDGDPITLD VEARRLTLEV SDEELDRRRR GWTPPPPHHK RGYGALFDAH
ILQADQGCDF DFLEGAGGPE PEVD
//
