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Database: UniProt
Entry: A0A239P9N5_9ACTN
LinkDB: A0A239P9N5_9ACTN
Original site: A0A239P9N5_9ACTN 
ID   A0A239P9N5_9ACTN        Unreviewed;       450 AA.
AC   A0A239P9N5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE            EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN   ORFNames=SAMN05216276_109722 {ECO:0000313|EMBL:SNT63109.1};
OS   Streptosporangium subroseum.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Streptosporangium.
OX   NCBI_TaxID=106412 {ECO:0000313|EMBL:SNT63109.1, ECO:0000313|Proteomes:UP000198282};
RN   [1] {ECO:0000313|EMBL:SNT63109.1, ECO:0000313|Proteomes:UP000198282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2132 {ECO:0000313|EMBL:SNT63109.1,
RC   ECO:0000313|Proteomes:UP000198282};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZOD01000097; SNT63109.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239P9N5; -.
DR   Proteomes; UP000198282; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000198282}.
FT   DOMAIN          214..310
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   450 AA;  49374 MW;  7D6C4DAF36DCC041 CRC64;
     MSERNEPTGA VASGTGEKGG DAYRITSMET HDIRFPTSLE LDGSDAMNPD PDYSAAYVVL
     KTDDGFEGHG FAFTIGRGNE VQTAAIRTLE SYVVGKDAED MGALWKDMVH DSQLRWLGPE
     KGVMHMAISA VVNALWDLKA KRVGKPLWLL LAEMSPEELV ALVDFRYLTD ALTPEQALDI
     LRAAEPGRQE RIAHLRERGY PAYTTSPGWL GYGDDKLRRL CKEAMAEGFT QIKLKVGADL
     EDDRRRMRIA RDTCGEDFPI AIDANQRWDV DSAIAWVNAL AEFRPHWVEE PTSPDDVLGH
     AAIARGIAPI PVATGEHVQN RVIFKQLLQA DAISYLQIDA ARVAGVNENI AILLLAAKFG
     VPVCPHAGGV GLCELVQHLS MFDYVAVSGS MENKVIEYVD HLHEHFIDPV VIKDGAYVAP
     SLPGFSAAMR ATSITDHTYP DGPVWRSLNG
//
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