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Database: UniProt
Entry: A0A367EXI7_9ACTN
LinkDB: A0A367EXI7_9ACTN
Original site: A0A367EXI7_9ACTN 
ID   A0A367EXI7_9ACTN        Unreviewed;       455 AA.
AC   A0A367EXI7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE            EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN   ORFNames=DTL70_14145 {ECO:0000313|EMBL:RCG22866.1};
OS   Streptomyces diacarni.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2800381 {ECO:0000313|EMBL:RCG22866.1, ECO:0000313|Proteomes:UP000252914};
RN   [1] {ECO:0000313|EMBL:RCG22866.1, ECO:0000313|Proteomes:UP000252914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW51701 {ECO:0000313|EMBL:RCG22866.1,
RC   ECO:0000313|Proteomes:UP000252914};
RA   Li L.;
RT   "Streptomyces reniochalinae sp. nov. and Streptomyces diacarnus sp. nov.
RT   from marine sponges.";
RL   Submitted (JUN-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   -!- 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:RCG22866.1}.
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DR   EMBL; QOIN01000043; RCG22866.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367EXI7; -.
DR   OrthoDB; 9796450at2; -.
DR   Proteomes; UP000252914; 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:UP000252914}.
FT   DOMAIN          203..299
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   455 AA;  49594 MW;  A1F0983F12D14DBE CRC64;
     MSADVARIIA MDTYDVRFPT SRQLDGSDAM NPDPDYSAAY VVLRTDAGEG LDGHGFTFTI
     GRGNDVQVAA IEALRGHVVG RPVAEVCADP GSLSRALTGD SQLRWLGPEK GVMHMAVGAV
     VNAAWDLAAR QARKPLWKLL ADAEPAWLVS QIDFRYLTDA LTEQEALDLL RHARTGREAR
     EEELHRGGYP AYTTSPGWLG YPDEKLARLA EEAMTAGFRQ IKLKVGADLE DDIRRCRTAR
     EVVGPGFRMA IDANQRWDVP EAIAWISRLA EFGPYWIEEP TSPDDVLGHA AIRRAVAPVK
     VATGEHVHNR VVFKQLLQAD AIDVLQLDAA RVGGVNENLA ILLLAAKFGV PVCPHAGGVG
     LCELVQHLSM FDFVAVSGTT EDRVIEYVDH LHEHFRDPVV IRDGHYAAPL TPGFSAAMSP
     ESIAAYTYPH GRFWAADLAR RGDGQGATDP AEVQA
//
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