ID A0A1A2L9B0_9MYCO Unreviewed; 568 AA.
AC A0A1A2L9B0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:OBG87383.1};
GN ORFNames=A5699_18980 {ECO:0000313|EMBL:OBG87383.1};
OS Mycobacterium sp. E802.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834152 {ECO:0000313|EMBL:OBG87383.1, ECO:0000313|Proteomes:UP000092062};
RN [1] {ECO:0000313|EMBL:OBG87383.1, ECO:0000313|Proteomes:UP000092062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E802 {ECO:0000313|EMBL:OBG87383.1,
RC ECO:0000313|Proteomes:UP000092062};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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:OBG87383.1}.
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DR EMBL; LZJD01000047; OBG87383.1; -; Genomic_DNA.
DR RefSeq; WP_067767578.1; NZ_LZJD01000047.1.
DR AlphaFoldDB; A0A1A2L9B0; -.
DR Proteomes; UP000092062; 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}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 59920 MW; DBBBF5F6000806DE CRC64;
MSESSGYQPG TSAVDSSRTS YGDAGFSRYL RRAFLASAGY DDESLERPII GIAVTQSDYN
TCHRDMPALL AAVKRGVEQA GGLPMDFPTI SLGEILTSPT TMLFRNLMAM DTEEMIRALP
MDAAVLLGGC DKTVPAQLMA AASSDIPVML EVVGPMMTGS WRGERLGACT DCRRFWGAHR
GGELDGDEIV SVRQELVSTT GTCTVMGTAS TMAALTEALG MMLPGGATPP AVSGARLRHA
TQTGRRAVEL ARTGGPLPRE VMTREAFENV IRVLAAIGGS TNALIHVIAV ARRAGVSLEL
ADFDKIGSDT PLLVDCKPSG AGYMEDFHRA GGVPALMTEL APLLHRDHRG VSGRSVGELI
ADTDGPAEWQ NTIRRRDDPL GPPGALAVLS GSLAPNGAII KASAASPHLM QHTGPALVVD
NPADASTILD DPDLDVTPEH VLVLRFSGPV AAGMPEAGAL PIPAKLARAG IRDMVRVSDA
RMSGTSYGTV VLHCDPEAAV GGPLSVVRNG DLIRLDVPNR SIDLLVPEEE IAERLRSFTP
PPRAARGWRR LYEETVLPAS QGADLSFL
//
