ID I3TQ70_TISMK Unreviewed; 576 AA.
AC I3TQ70;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:AFK54908.1};
GN OrderedLocusNames=TMO_3070 {ECO:0000313|EMBL:AFK54908.1};
OS Tistrella mobilis (strain KA081020-065).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK54908.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK54908.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK54908.1,
RC ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; CP003236; AFK54908.1; -; Genomic_DNA.
DR RefSeq; WP_014746585.1; NC_017956.1.
DR AlphaFoldDB; I3TQ70; -.
DR STRING; 1110502.TMO_3070; -.
DR KEGG; tmo:TMO_3070; -.
DR PATRIC; fig|1110502.3.peg.3148; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_3_1_5; -.
DR Proteomes; UP000005258; 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: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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258}.
SQ SEQUENCE 576 AA; 63012 MW; 3C1A1FFFB728F655 CRC64;
MTRTYDELRS ARWFAPDNFR GFGHRSRTLQ MGYDEQDWAG KPVVAILNTW SDINPCHQHF
RQRVDDVKRG VFQAGGFPIE LPALSVSENY VKPTTMLYRN MLAMETEELI RSHPVDGVVL
MGGCDKTTPG LVMGAISAGL PAIYLPAGPM LRGNWEGRTL GSGSDAFKYW DERRAGTITE
AQWKGMERGI ARSYGHCMTM GTASTMTAIA EALGLTLPGA SSIPAADSNH IRMSADCGRR
IVGMIWEDLT PARILTAAAF DNAVTVAMAT GCSTNAVVHL IAMARRAGVD LTLDDLDAKS
RVTPVIANIR PAGSTYLMED FFYAGGLRAL MARLGDRLHR DCLTVTGRTL GEGIDGAEVW
NDDVIRTVDN PIYNEGSLAV LKGNLAPDGA VIKPVACDPR FLVHEGPAIV FDSYPELKEK
LDDEDWDITP DAVLVLRNAG PKGGPGMPEW GMIPMPKALL KQGCRDMVRL SDARMSGTSF
GACVLHVAPE SYVGGPLALL QTGDIVRLDV PGRRLDMLVD DEEIARRRAA WTPPPPRFHR
GWGWMFTNHI QQADKGCDFD YLETSFGAPV DEPVIY
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