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Database: UniProt
Entry: A0A0X3W7D9_9ACTN
LinkDB: A0A0X3W7D9_9ACTN
Original site: A0A0X3W7D9_9ACTN 
ID   A0A0X3W7D9_9ACTN        Unreviewed;       466 AA.
AC   A0A0X3W7D9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE            EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN   ORFNames=ADL30_22330 {ECO:0000313|EMBL:KUL52850.1};
OS   Streptomyces sp. NRRL S-1521.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609100 {ECO:0000313|EMBL:KUL52850.1, ECO:0000313|Proteomes:UP000053420};
RN   [1] {ECO:0000313|EMBL:KUL52850.1, ECO:0000313|Proteomes:UP000053420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL S-1521 {ECO:0000313|EMBL:KUL52850.1,
RC   ECO:0000313|Proteomes:UP000053420};
RA   Gilbert D.G.;
RL   Submitted (OCT-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:KUL52850.1}.
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DR   EMBL; LLZK01000212; KUL52850.1; -; Genomic_DNA.
DR   RefSeq; WP_062778094.1; NZ_LLZK01000212.1.
DR   AlphaFoldDB; A0A0X3W7D9; -.
DR   Proteomes; UP000053420; Unassembled WGS sequence.
DR   GO; GO:0050023; F:L-fuconate dehydratase activity; IEA:UniProtKB-EC.
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; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053420}.
FT   DOMAIN          203..299
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   REGION          444..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   466 AA;  49940 MW;  1E1DF2F47D715914 CRC64;
     MPPTPARITA VDTYDIRFPT SRELDGSDAM NPDPDYSAAY VVLRTDAGDG IEGHGFTFTI
     GRGNDVQVAA IRALRHHVTG RAVDEVCADP GTVNRALVGD SQLRWLGPEK GVMHMAIGAV
     VNAVWDLAAK RAGKPLWQLL ADATPEWLVS QVDFRYIADA LTPEDALALL RQGRRGAAAR
     EAVLRERGFP GYTTSPGWLG YSDAKLTRLA RAAVADGFTQ IKLKVGADLA DDIRRCRTAR
     EAIGPGVRMA IDANQRWNVD EAVAWTRALA EFDPYWVEEP TSPDDVLGHA AIRAAVAPVK
     VATGEHVQNR VVFKQLLQAG AIDVLQIDAA RVGGVNENLA ILLLAARFGV PVCPHAGGVG
     LCELVQHLSM FDYVALAGTT ENRVIEYVDH LHEHFTDPVV MRAGHYTPPT APGFSATMRA
     ESIAGFTYPD GTFWTADLAQ ADHTQADHAS AGPAPADLAP DKGAAA
//
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