ID A0A0M2H8T1_9MICO Unreviewed; 431 AA.
AC A0A0M2H8T1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN ORFNames=RS82_01791 {ECO:0000313|EMBL:KJL42826.1};
OS Microbacterium trichothecenolyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL42826.1, ECO:0000313|Proteomes:UP000034098};
RN [1] {ECO:0000313|EMBL:KJL42826.1, ECO:0000313|Proteomes:UP000034098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL42826.1,
RC ECO:0000313|Proteomes:UP000034098};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL42826.1}.
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DR EMBL; JYJA01000033; KJL42826.1; -; Genomic_DNA.
DR RefSeq; WP_045298457.1; NZ_JYJA01000033.1.
DR AlphaFoldDB; A0A0M2H8T1; -.
DR PATRIC; fig|69370.6.peg.1822; -.
DR OrthoDB; 9796450at2; -.
DR Proteomes; UP000034098; 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 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:0000313|EMBL:KJL42826.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034098}.
FT DOMAIN 199..295
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 431 AA; 46638 MW; 652811588354A2F4 CRC64;
MSRIVAFETT DIRFPTSLSL DGSDAMNPDP DYSAAYLRIV TDAADHVSGH AFVFTIGRGN
DVQVAALDAL AAHLVGRELE PLLDEMGAIN RELIGDSQLR WLGPEKGVMH MAIGAVVNAL
WDIKAKRAGL PLWQLLSRMS PEELVALVDF RYLSNALTPE DALRILRDAE PGRAERESEL
LATGYPAYTT SPGWLGYSDE KLARLCREAI ADGFGQIKLK VGADLDDDIR RLRVARAVCG
EGFPIAIDAN QRWEVSEAIE WVNALAEFDP AWIEEPTSPD DVLGHAEIAR GIAPVRVATG
EHAQNRVIFK QLLQAGAISV MQIDAARVGG VNENIANLLL AAKFGVPVCP HAGGVGLCEA
VQHLSMFDFV AVTGTREGRM IEYVDHLHEH FVVPTEVRGG VYVAPTAPGT GMEMKAASRA
EYEFGTAHAA A
//
