ID A0A0X3W7D9_9ACTN Unreviewed; 466 AA.
AC A0A0X3W7D9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN ORFNames=ADL30_22330 {ECO:0000313|EMBL:KUL52850.1};
OS Streptomyces sp. NRRL S-1521.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609100 {ECO:0000313|EMBL:KUL52850.1, ECO:0000313|Proteomes:UP000053420};
RN [1] {ECO:0000313|EMBL:KUL52850.1, ECO:0000313|Proteomes:UP000053420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-1521 {ECO:0000313|EMBL:KUL52850.1,
RC ECO:0000313|Proteomes:UP000053420};
RA Gilbert D.G.;
RL Submitted (OCT-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:KUL52850.1}.
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; LLZK01000212; KUL52850.1; -; Genomic_DNA.
DR RefSeq; WP_062778094.1; NZ_LLZK01000212.1.
DR AlphaFoldDB; A0A0X3W7D9; -.
DR Proteomes; UP000053420; 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:UP000053420}.
FT DOMAIN 203..299
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
FT REGION 444..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 49940 MW; 1E1DF2F47D715914 CRC64;
MPPTPARITA VDTYDIRFPT SRELDGSDAM NPDPDYSAAY VVLRTDAGDG IEGHGFTFTI
GRGNDVQVAA IRALRHHVTG RAVDEVCADP GTVNRALVGD SQLRWLGPEK GVMHMAIGAV
VNAVWDLAAK RAGKPLWQLL ADATPEWLVS QVDFRYIADA LTPEDALALL RQGRRGAAAR
EAVLRERGFP GYTTSPGWLG YSDAKLTRLA RAAVADGFTQ IKLKVGADLA DDIRRCRTAR
EAIGPGVRMA IDANQRWNVD EAVAWTRALA EFDPYWVEEP TSPDDVLGHA AIRAAVAPVK
VATGEHVQNR VVFKQLLQAG AIDVLQIDAA RVGGVNENLA ILLLAARFGV PVCPHAGGVG
LCELVQHLSM FDYVALAGTT ENRVIEYVDH LHEHFTDPVV MRAGHYTPPT APGFSATMRA
ESIAGFTYPD GTFWTADLAQ ADHTQADHAS AGPAPADLAP DKGAAA
//