ID A0A1M7NLM7_9ACTN Unreviewed; 432 AA.
AC A0A1M7NLM7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN ORFNames=SAMN05216499_11944 {ECO:0000313|EMBL:SHN04896.1};
OS Actinacidiphila paucisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310782 {ECO:0000313|EMBL:SHN04896.1, ECO:0000313|Proteomes:UP000184111};
RN [1] {ECO:0000313|EMBL:SHN04896.1, ECO:0000313|Proteomes:UP000184111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2025 {ECO:0000313|EMBL:SHN04896.1,
RC ECO:0000313|Proteomes:UP000184111};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FRBI01000019; SHN04896.1; -; Genomic_DNA.
DR RefSeq; WP_073501200.1; NZ_FRBI01000019.1.
DR AlphaFoldDB; A0A1M7NLM7; -.
DR STRING; 310782.SAMN05216499_11944; -.
DR OrthoDB; 9796450at2; -.
DR Proteomes; UP000184111; 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 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:UP000184111}.
FT DOMAIN 198..294
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 432 AA; 47344 MW; F005851A51949A55 CRC64;
MADLITALEA HDIRFPTSQH LDGSDALNPE PDYSAAYAVL RTSGDEEGYG LAFTVGRGNE
VQVAAIRALE PLVVGLDVQE VLGNLGAFSR LLTGDSQLRW LGPHKGVVHM AAAAVVNAAW
DLFGRREGLP VWRLLSRMSP EQLVDLVDFR YLRDALTPEE ALAILRRAAP GRQEREEQLL
RTGYPAYTTT PGWLGYSDDK LLRLSKEAVA DGFTQIKLKV GANREDDVRR MALAREAVGA
DIRIAVDSNQ AWGVQEAIEW MRLLAPHNPY WIEEPTSPDD ILGHAAVRRA VAPIKVATGE
HCHNQVMFKQ LLQADAIDVL QMDASRVAGV TENVAILLLA AKFGVPVCPH AGGVGLCEMV
QHLSMFDYVA VSGSTEDRTI EYVDHLHEHF EDPVVVRNGR YAAPLSPGLG ARLLPQSAAD
HRFPDGPVWR NA
//