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Database: UniProt
Entry: A0A1Y6CTU7_9PROT
LinkDB: A0A1Y6CTU7_9PROT
Original site: A0A1Y6CTU7_9PROT 
ID   A0A1Y6CTU7_9PROT        Unreviewed;       586 AA.
AC   A0A1Y6CTU7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:SMF76534.1};
GN   ORFNames=SAMN05428998_13562 {ECO:0000313|EMBL:SMF76534.1};
OS   Tistlia consotensis USBA 355.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Fodinicurvataceae; Tistlia.
OX   NCBI_TaxID=560819 {ECO:0000313|EMBL:SMF76534.1, ECO:0000313|Proteomes:UP000192917};
RN   [1] {ECO:0000313|EMBL:SMF76534.1, ECO:0000313|Proteomes:UP000192917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USBA 355 {ECO:0000313|EMBL:SMF76534.1,
RC   ECO:0000313|Proteomes:UP000192917};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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; FWZX01000035; SMF76534.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6CTU7; -.
DR   STRING; 560819.SAMN05428998_13562; -.
DR   Proteomes; UP000192917; 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: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:UP000192917}.
SQ   SEQUENCE   586 AA;  63006 MW;  21792BF96AFF6A78 CRC64;
     MTAETKRNSL ARKAPGKLRS ARWFAPDDLR SFGHRSRAMQ MGYAPEDWAG KPVVAIVNTW
     SDAQPCHAHF KSRVEDVKRG VFQAGGFPME LPALSLSESF VKPTTMLYRN MLAMETEELL
     RSHPVDAAVL MGGCDKTTPG LVMGALSAGL PMIFLPAGPM LRGNYRGQAL GSGSDAWKYW
     DERRAGNLSA AEWQGVEGGI ARSYGHCMTM GTASTMTAIA EALGLTLSGA SSIPAADANH
     IRMASAVGRR AVEMAWEDLT PDRVLDARAV RNAVTVAMAT GCSTNAVIHL IAMARRAGVP
     LGLDDLDAAS RVTPVIANIR PSGSTYLMED FYYAGGLRAL MARLGDRLDL SAVTVSGRTL
     GEELEGAEVY DEDVIRSLEN PIYQEGSLAV LRGNLAPDGC VIKPSACAPH LRQHEGRALV
     FDSYPGMKAA VEDESLDVTA DDVLVLRNAG PRGGPGMPEW GMLPIPKKLV KEGVRDMLRI
     SDARMSGTSY GACVLHVAPE ACVGGPLALL RTGDRIRVDV PARTIDMLVE PEELARRRAA
     WTPPAETVGR GWNWLFARHI EQADQGCDFD FLKSGFGASA GEPDIF
//
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