ID A0A0T1WCD9_9MYCO Unreviewed; 445 AA.
AC A0A0T1WCD9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN ORFNames=ASD37_11455 {ECO:0000313|EMBL:KQY06771.1};
OS Mycobacterium sp. Root135.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1736457 {ECO:0000313|EMBL:KQY06771.1, ECO:0000313|Proteomes:UP000051127};
RN [1] {ECO:0000313|EMBL:KQY06771.1, ECO:0000313|Proteomes:UP000051127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root135 {ECO:0000313|EMBL:KQY06771.1,
RC ECO:0000313|Proteomes:UP000051127};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY06771.1, ECO:0000313|Proteomes:UP000051127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root135 {ECO:0000313|EMBL:KQY06771.1,
RC ECO:0000313|Proteomes:UP000051127};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQY06771.1}.
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DR EMBL; LMEZ01000005; KQY06771.1; -; Genomic_DNA.
DR RefSeq; WP_056551200.1; NZ_LMEZ01000005.1.
DR AlphaFoldDB; A0A0T1WCD9; -.
DR STRING; 1736457.ASD37_11455; -.
DR OrthoDB; 5241672at2; -.
DR Proteomes; UP000051127; 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 GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-KW.
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; 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 Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428};
KW Reference proteome {ECO:0000313|Proteomes:UP000051127}.
FT DOMAIN 198..293
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 445 AA; 48528 MW; 2B7765224CA9ECEF CRC64;
MTRITSVDVT DVRFPTSLSM DGSDAMNKDG DYSATYVVLR TDDPRLAGYG FTFTIGRGND
ICTLAARQRA EPLVGRDVAG MVGDLGGTYR DLAGDSQLRW LGPDKGVEHL AMAAVMNAVW
DLAARVAGKP LWRLLSEMDT EDLVDTLDLT YLSDVLTRQE AVDMLAESVP TRAARIADMD
RTGYPCYTTS AGWLGYSDDK LRELAALAVA DGYRHVKLKV GANLADDIRR CTIAREVIGW
DAHLMIDANQ VWDVPEAIEW VNALAKFKPL WIEEPTSPDD VLGHAAVRKA VVPIGVATGE
HGMNRVLFKQ LFQAEAIDYC QLDAARLASI NEIIPVYLMA KKFGVPVCPH AGGVGLCELV
QHLSVFDYVA VAGTTENRVT EFVDHLHEHF TDPCVVESGA YVLPTKPGYS AQMYAASVAE
YAYPDGAYWS TRHPHAVVVS EAGVG
//