ID A0A2R8BR81_9RHOB Unreviewed; 424 AA.
AC A0A2R8BR81;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN ORFNames=PAA8504_00433 {ECO:0000313|EMBL:SPJ22638.1};
OS Palleronia abyssalis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Palleronia.
OX NCBI_TaxID=1501240 {ECO:0000313|EMBL:SPJ22638.1, ECO:0000313|Proteomes:UP000244912};
RN [1] {ECO:0000313|EMBL:SPJ22638.1, ECO:0000313|Proteomes:UP000244912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8504 {ECO:0000313|EMBL:SPJ22638.1,
RC ECO:0000313|Proteomes:UP000244912};
RA Keele B.F.;
RL Submitted (MAR-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ONZF01000001; SPJ22638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8BR81; -.
DR OrthoDB; 9802699at2; -.
DR Proteomes; UP000244912; Unassembled WGS sequence.
DR GO; GO:0050023; F:L-fuconate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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;
KW Lyase {ECO:0000313|EMBL:SPJ22638.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244912}.
FT DOMAIN 196..292
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 424 AA; 47387 MW; 17B410AB5791DF2D CRC64;
MRITGLRTAD VRFPTSDALD GSDAMNPDPD YSAAYVVLET DGDHDGHGLT FTIGRGNEIC
VAAIEALRPL VVGLDLDWIA EDMGRFWRHV TGDSQLRWIG PDKGAIHLAT GAVINAAWDL
WAKSQGKPVW QLVADMGPED LVRCIDFRYI TDCVTPDWAV AFLTRQSEGK ADRIATLMAE
GYPCYTTSAG WLGYDDEKLR RLCREVVDQG FRHIKMKVGR DLQDDIRRLR IARETVGPDV
QLMIDANQVW EVDQAVEWIN ALGFAQPWFI EEPTSPDDVA GHRAIRQAVA PVQVATGEMC
QNRIMFKQFI MQNAIDVVQI DSCRLGGLNE VLAVMLMAAK YDLLVCPHAG GVGLCEYVQH
MSMIDYLCIA GTREGRVIEY VDHLHEHFVD PCVIQNAAYM PPRRPGFSIE MKPESVAQFS
FGRT
//