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Database: UniProt
Entry: A0A1M6KDB6_9BURK
LinkDB: A0A1M6KDB6_9BURK
Original site: A0A1M6KDB6_9BURK 
ID   A0A1M6KDB6_9BURK        Unreviewed;       432 AA.
AC   A0A1M6KDB6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE            EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN   ORFNames=SAMN05192548_1003183 {ECO:0000313|EMBL:SHJ56857.1};
OS   Paraburkholderia terricola.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=169427 {ECO:0000313|EMBL:SHJ56857.1, ECO:0000313|Proteomes:UP000184395};
RN   [1] {ECO:0000313|EMBL:SHJ56857.1, ECO:0000313|Proteomes:UP000184395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20594 {ECO:0000313|EMBL:SHJ56857.1,
RC   ECO:0000313|Proteomes:UP000184395};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-fuconate = 2-dehydro-3-deoxy-L-fuconate + H2O;
CC         Xref=Rhea:RHEA:22772, ChEBI:CHEBI:15377, ChEBI:CHEBI:21291,
CC         ChEBI:CHEBI:37448; EC=4.2.1.68;
CC         Evidence={ECO:0000256|ARBA:ARBA00001737};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; FRAB01000003; SHJ56857.1; -; Genomic_DNA.
DR   RefSeq; WP_073427404.1; NZ_JAVDRP010000001.1.
DR   AlphaFoldDB; A0A1M6KDB6; -.
DR   STRING; 169427.SAMN05192548_1003183; -.
DR   KEGG; pts:CUJ90_27840; -.
DR   OrthoDB; 8609034at2; -.
DR   Proteomes; UP000184395; Unassembled WGS sequence.
DR   GO; GO:0050023; F:L-fuconate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009063; P:amino acid catabolic process; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR   CDD; cd03324; rTSbeta_L-fuconate_dehydratase; 1.
DR   Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1.
DR   Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR029065; Enolase_C-like.
DR   InterPro; IPR034610; L-fuconate_dehydratase.
DR   InterPro; IPR018110; Mandel_Rmase/mucon_lact_enz_CS.
DR   InterPro; IPR013342; Mandelate_racemase_C.
DR   InterPro; IPR013341; Mandelate_racemase_N_dom.
DR   InterPro; IPR046945; RHMD-like.
DR   PANTHER; PTHR13794; ENOLASE SUPERFAMILY, MANDELATE RACEMASE; 1.
DR   PANTHER; PTHR13794:SF58; MITOCHONDRIAL ENOLASE SUPERFAMILY MEMBER 1; 1.
DR   Pfam; PF13378; MR_MLE_C; 1.
DR   Pfam; PF02746; MR_MLE_N; 1.
DR   SFLD; SFLDF00111; L-fuconate_dehydratase; 1.
DR   SFLD; SFLDG00179; mandelate_racemase; 1.
DR   SMART; SM00922; MR_MLE; 1.
DR   SUPFAM; SSF51604; Enolase C-terminal domain-like; 1.
DR   SUPFAM; SSF54826; Enolase N-terminal domain-like; 1.
DR   PROSITE; PS00909; MR_MLE_2; 1.
PE   4: Predicted;
FT   DOMAIN          199..295
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   432 AA;  48259 MW;  A38981790458C2ED CRC64;
     MTTITNLSVR DIRFPTSRSL DGSDAMNAAP DYSAAYVVLE TDSPEQFAGH GLTFTIGRGN
     EICVTAVNAL APLVVGKTLE AIVADMGSFW RAFTSDSQLR WIGPDKGAIH LATAAVVNAV
     WDLWAKTERK PVWKLLVDMS PEALVRCLDF RYVTDALTPH EALAILRRHA ATRGEREAQM
     LAHGYPAYTT SAGWLGYDDE KIRRLAREGV AQGWTHFKQK VGGNLDEDVR RARILRDEIG
     ADRKLMMDAN QVWEVDEAIA NMRRLAEFDP WWIEEPTSPD DILGHAAIRR RVAPIGVATG
     EHCHNRVMFK QLLQAQAIDF CQVDSCRLGG LNEVLVVLLM AAKFGVPVCP HAGGVGLCEY
     VQHISLFDYI CVSASLENRV LEYVDHLHEH FVDPVVIRNG RYMPPQQPGY SIEMRAESLE
     QFHFPQGAAW RV
//
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