ID E8V801_TERSS Unreviewed; 434 AA.
AC E8V801;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN OrderedLocusNames=AciPR4_2122 {ECO:0000313|EMBL:ADV82925.1};
OS Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV82925.1, ECO:0000313|Proteomes:UP000006844};
RN [1] {ECO:0000313|EMBL:ADV82925.1, ECO:0000313|Proteomes:UP000006844}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4
RC {ECO:0000313|Proteomes:UP000006844};
RX PubMed=23450133; DOI=10.4056/sigs.3036810;
RA Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., Hauser L.,
RA Land M., Davenport K.W., Woyke T., Haggblom M.M.;
RT "Complete genome sequence of Terriglobus saanensis type strain SP1PR4(T),
RT an Acidobacteria from tundra soil.";
RL Stand. Genomic Sci. 7:59-69(2012).
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; CP002467; ADV82925.1; -; Genomic_DNA.
DR RefSeq; WP_013568658.1; NC_014963.1.
DR AlphaFoldDB; E8V801; -.
DR STRING; 401053.AciPR4_2122; -.
DR KEGG; tsa:AciPR4_2122; -.
DR eggNOG; COG4948; Bacteria.
DR HOGENOM; CLU_030273_2_0_0; -.
DR OrthoDB; 9775391at2; -.
DR Proteomes; UP000006844; Chromosome.
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; 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.
DR PROSITE; PS00909; MR_MLE_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006844}.
FT DOMAIN 199..295
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 434 AA; 49246 MW; DF163C3FD3A96FAB CRC64;
MQSIVIERVR VVDLRFPTSR ESIGSDAVNK DPDYSAAYCI LETNSEVEGH GLTFTLGRGT
DLVVQALEYL SKFAVGRTLD SITENFAKFS RELTDESQFR WLGPEKGVIH LATGALINAV
WDLYAKVEGK PLWRLLAEME PEQLLKAVEF RYIDDALTYD EALAILQRGR EGKAERMEQL
LEHGYPAYTT SVGWFGFSDE KVRRLCREAL ADGWTHFKLK VGGDAVDDLR RGRLVREEIG
WTNKLMVDAN QKWGVLEAIE RTKQLAELQP WWMEEPTNPD DILGHARIRR EAAPVPIATG
EHCQNRVMFK QLMQAEAIDV CQIDSCRVAG VNENLAIILL AAKFGVRVCP HAGGVGLCEY
VQHLSMFDYL CVSTTMKDRV IEFVDHLHEH FVDPVRIRRG HYLAPENPGY SIAVFPSTIT
KYSFPDGEVW KEEQ
//
