ID A0A3S0J1P6_9BURK Unreviewed; 425 AA.
AC A0A3S0J1P6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN ORFNames=EJP69_12280 {ECO:0000313|EMBL:RTQ35156.1};
OS Variovorax gossypii.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Comamonadaceae; Variovorax.
OX NCBI_TaxID=1679495 {ECO:0000313|EMBL:RTQ35156.1, ECO:0000313|Proteomes:UP000267418};
RN [1] {ECO:0000313|EMBL:RTQ35156.1, ECO:0000313|Proteomes:UP000267418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100435 {ECO:0000313|EMBL:RTQ35156.1,
RC ECO:0000313|Proteomes:UP000267418};
RA Gao J., Sun J.;
RT "The genome of Variovorax gossypii DSM 100435.";
RL Submitted (DEC-2018) 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};
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:RTQ35156.1}.
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DR EMBL; RXOE01000002; RTQ35156.1; -; Genomic_DNA.
DR RefSeq; WP_126470333.1; NZ_RXOE01000002.1.
DR AlphaFoldDB; A0A3S0J1P6; -.
DR OrthoDB; 8609034at2; -.
DR Proteomes; UP000267418; Unassembled WGS sequence.
DR GO; GO:0050023; F:L-fuconate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:TreeGrafter.
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 FunFam; 3.20.20.120:FF:000007; Mitochondrial enolase superfamily member 1; 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; SFLDS00001; Enolase; 1.
DR SFLD; SFLDF00111; L-fuconate_dehydratase; 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;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000267418}.
FT DOMAIN 198..294
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 425 AA; 47667 MW; 8D68E4C9F1819745 CRC64;
MTIVRSMRVL DVRFPTSQHL DGSDAMNPDP DYSAAYVVLE TDRPGLEGHG LTFTIGRGNE
ICCAAIEAMR HLVVGLDLAW VAEDMGRFWR HVTSDSQLRW IGPDKGAIHL ATGAVVNAMW
DLWAKSEGKP VWQLVADMSP EELVRCIDFR YITDCIAPDE ALALLREASR GKEERIATLK
AGGYPCYTTS AGWLGYSDDK LRRLAQEAID AGFSHIKLKV GRDLQDDIRR LTVAREVLGP
ERHLMIDANQ VWEVGQAIDW VRQLAFARPW FIEEPTSPDD VEGHRKIREG ISPVKVATGE
MCQNRIMFKQ FIMRGGIDVV QIDACRLGGV NEILAVMLMA AKYRLPVCPH AGGVGLCEYV
QHLSMIDYLC ISGTREGRVA EYVDHLHEHF VEPCEIRNAA YMPPKGPGFS ITMKPQSLEQ
YRFRG
//
