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Database: UniProt
Entry: A0A0F0HV61_9PSEU
LinkDB: A0A0F0HV61_9PSEU
Original site: A0A0F0HV61_9PSEU 
ID   A0A0F0HV61_9PSEU        Unreviewed;       455 AA.
AC   A0A0F0HV61;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE            EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN   ORFNames=UK12_15680 {ECO:0000313|EMBL:KJK57588.1};
OS   Saccharothrix sp. ST-888.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK57588.1, ECO:0000313|Proteomes:UP000033409};
RN   [1] {ECO:0000313|EMBL:KJK57588.1, ECO:0000313|Proteomes:UP000033409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST-888 {ECO:0000313|EMBL:KJK57588.1,
RC   ECO:0000313|Proteomes:UP000033409};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
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:KJK57588.1}.
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DR   EMBL; JYJF01000042; KJK57588.1; -; Genomic_DNA.
DR   RefSeq; WP_045303587.1; NZ_JYJF01000042.1.
DR   AlphaFoldDB; A0A0F0HV61; -.
DR   PATRIC; fig|1427391.3.peg.4732; -.
DR   Proteomes; UP000033409; 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; 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:UP000033409}.
FT   DOMAIN          207..303
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   455 AA;  49392 MW;  1174B320B1FA5CE3 CRC64;
     MKGTTLPATT ARITAVDTYD IRFPTSRELD GSDAMNPDPD YSAAYVVLRT SAGGHEGHGF
     TFTIGRGNDV QVAAIDALRE HIVGRPVAEL CADPGSLYRD LIGDSQLRWL GPEKGVMHMA
     IGAVVNAVWD LAAKREGKPL WQLLADADPD WLVSQVDFRY IADALTPDEA LELLAKGKQG
     AGERAAELLR RGYPAYTTSP GWLGYSDEKL TRLAEQAVAD GFTQIKLKVG ADLEDDIRRC
     RAARAAVGPD IRMAIDANQR WNVAEAIEWT NALAEFDPYW IEEPTSPDDV LGHAAVRQGV
     HPIKVATGEH VQNRIVFKQL LQAGAIDVLQ LDSARVAGVN ENLAILLLAA KFGVPVCPHA
     GGVGLCELVQ HLSMFDYVAL SGTIEDRVVE YVDHLHQHFL DPVVINSGRY RAPTVPGFSA
     TMHQATIDTY TYPDGAFWAA DTAADLCGAD TEERA
//
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