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Database: UniProt
Entry: A0A0B5IIC1_9ACTN
LinkDB: A0A0B5IIC1_9ACTN
Original site: A0A0B5IIC1_9ACTN 
ID   A0A0B5IIC1_9ACTN        Unreviewed;       447 AA.
AC   A0A0B5IIC1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE            EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN   ORFNames=SVTN_37145 {ECO:0000313|EMBL:AJF70237.1};
OS   Streptomyces vietnamensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=362257 {ECO:0000313|EMBL:AJF70237.1, ECO:0000313|Proteomes:UP000031774};
RN   [1] {ECO:0000313|EMBL:AJF70237.1, ECO:0000313|Proteomes:UP000031774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GIMV4.0001 {ECO:0000313|Proteomes:UP000031774};
RA   Deng M.R., Guo J., Ma L.Y., Feng G.D., Mo C.Y., Zhu H.H.;
RT   "Complete genome sequence of Streptomyces vietnamensis strain GIMV4.0001, a
RT   genetic manipulable producer of the benzoisochromanequinone antibiotic
RT   granaticin.";
RL   Submitted (DEC-2014) 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};
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DR   EMBL; CP010407; AJF70237.1; -; Genomic_DNA.
DR   RefSeq; WP_041134667.1; NZ_CP010407.1.
DR   AlphaFoldDB; A0A0B5IIC1; -.
DR   STRING; 362257.SVTN_37145; -.
DR   KEGG; svt:SVTN_37145; -.
DR   HOGENOM; CLU_030273_2_0_11; -.
DR   Proteomes; UP000031774; Chromosome.
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; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000031774}.
FT   DOMAIN          203..299
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   447 AA;  48834 MW;  FB8C959945C89D79 CRC64;
     MPDPTARITS IDTYDVRFPT SRELDGSDAM NPDPDYSAAY LVLRTSAADG HEGHGFTFTI
     GRGNDVQVAA IDALRGHVVG RSVVELCADP GVLYRDLVGD SQLRWLGPEK GVMHMAIGAV
     VNAVWDLAAK REGKPLWRLL ADAAPAWLVS QVDFRYLTDA LTPDEALELL TKGKQGAAER
     AADLLRRGYP AYTTSPGWLG YSDEKLTRLA EEAVADGFTQ IKLKVGADLD DDIRRCRTAR
     AAVGPDIRMA IDANQRWDVA EAVEWTNALA EFDPYWIEEP TSPDDVLGHA AVRRGVHPVK
     VATGEHVQNR IVFKQLLQAE AVDFLQLDAA RVAGVNENLA ILLLAAKFGV PVCPHAGGVG
     LCELVQHLSM FDYVALSGTT EDRVVEFVDH LHEHFLDPVM IDRGHYRAPT EPGFSATMRQ
     SSLDAYRYPD GAFWAADLAA PTPEARA
//
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