ID L9M6T1_9GAMM Unreviewed; 425 AA.
AC L9M6T1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, 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=ACINWC743_3586 {ECO:0000313|EMBL:ELW82955.1};
OS Acinetobacter sp. WC-743.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=903945 {ECO:0000313|EMBL:ELW82955.1, ECO:0000313|Proteomes:UP000011515};
RN [1] {ECO:0000313|EMBL:ELW82955.1, ECO:0000313|Proteomes:UP000011515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WC-743 {ECO:0000313|EMBL:ELW82955.1,
RC ECO:0000313|Proteomes:UP000011515};
RA Harkins D.M., Brinkac L.M., Durkin A.S., Beck E., Fedorova N.B., Kim M.,
RA Onuska J., Radune D., DePew J., Koroleva G.I., Singh I., Chahine M.A.,
RA Cash D.M., Huang X.-Z., Nikolich M.P., Nierman W.C., Fouts D.E.;
RL Submitted (SEP-2012) 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:ELW82955.1}.
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DR EMBL; AMFQ01000090; ELW82955.1; -; Genomic_DNA.
DR RefSeq; WP_009585760.1; NZ_AMFQ01000090.1.
DR AlphaFoldDB; L9M6T1; -.
DR PATRIC; fig|903945.3.peg.2510; -.
DR Proteomes; UP000011515; 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 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;
FT DOMAIN 198..294
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 425 AA; 48179 MW; 9FFD7F0C197091A5 CRC64;
MLKITDLEVL DIRFPTSQQL DGSDAMNPDP DYSAAYVILK TDRPALTGHG LTFTIGRGNE
ICCAAIEAMR HLVVGLDIDE IKKNPALMWR HLTSDSQLRW IGPDKGAMHL ATGAVVNAIW
DLWAKSEAKP VWKLVADMTP EQLVNCIDFR YLTDCITPDE ALNLLKSNEI GKAQREKTLL
EEGYPCYTTS AGWLGYSDEK LARLCQEAVD EGFNYIKLKV GRDVEEDKRR VKIAREIIGP
DRHLMIDANQ IWEREQAIEW VKQLAFSNPW FIEEPTSPDD VEAHRAIRFA IQPIQVATGE
MCQNRIMFKQ FIMREAIDIV QIDACRMGGI NEVLAVLLMA AKYKLKVCPH AGGVGLCEYV
QHLSMIDYLW FSTSKEGRVT EYVDHLHEHF IDPCVIQNAA YMPPTLAGFS IEMKPASIEK
YRFKG
//