ID   A0A239EQ15_9BACT        Unreviewed;       444 AA.
AC   A0A239EQ15;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE            EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN   ORFNames=SAMN05421770_1011104 {ECO:0000313|EMBL:SNS46850.1};
OS   Granulicella rosea.
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Granulicella.
OX   NCBI_TaxID=474952 {ECO:0000313|EMBL:SNS46850.1, ECO:0000313|Proteomes:UP000198356};
RN   [1] {ECO:0000313|EMBL:SNS46850.1, ECO:0000313|Proteomes:UP000198356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18704 {ECO:0000313|EMBL:SNS46850.1,
RC   ECO:0000313|Proteomes:UP000198356};
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FZOU01000001; SNS46850.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239EQ15; -.
DR   OrthoDB; 9775391at2; -.
DR   Proteomes; UP000198356; 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   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:UP000198356}.
FT   DOMAIN          199..295
FT                   /note="Mandelate racemase/muconate lactonizing enzyme C-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00922"
SQ   SEQUENCE   444 AA;  49575 MW;  A232A5D979EF6B87 CRC64;
     MKATTITGAR VIDLRFPTSL HHIGSDAVNK DPDYSAAYCI LETDGELEGH GLTFTLGRGT
     ELCVAALEYL TKFVVGRTLD SIAKDLNAFY LEVTGDTQFR WLGPEKGVIH LACGALINAV
     WDLYAKAEDK PVWKLLADMT PEQIVAAVDF RYIADALSPA EALELLRRGK AGQAERLARL
     ESEGYPAYTT SAGWFGFSDE KIRRLCHEGL ADGWTKFKLK VGGDAADDLR RGRIVREEIG
     WKNRMMVDAN QRWGVEEAIA RTRQLAELQP WWMEEPTSPD DILGHARIRR EVRPVRIATG
     EHCQNAVMFK QLLQAEAIDV CQIDSCRVAG VNENLAILLM AAKFGVPVCP HAGGVGLCEY
     VQHLSIFDFL GVSCTLEDRV IEYVDHLHEH FRDPVKIRRG HYLVPRMAGY SCEILPESLA
     EFAYPGGSVW RKMSEEKRLA GVSQ
//