ID A0A229X2H1_9EURO Unreviewed; 451 AA.
AC A0A229X2H1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 03-MAY-2023, entry version 23.
DE RecName: Full=L-fuconate dehydratase {ECO:0000256|ARBA:ARBA00013142};
DE EC=4.2.1.68 {ECO:0000256|ARBA:ARBA00013142};
GN Name=LGD1 {ECO:0000313|EMBL:RHZ71322.1};
GN ORFNames=CDV55_108615 {ECO:0000313|EMBL:RHZ71322.1}, CFD26_108501
GN {ECO:0000313|EMBL:RLM01438.1};
OS Aspergillus turcosus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1245748 {ECO:0000313|EMBL:RHZ71322.1, ECO:0000313|Proteomes:UP000215394};
RN [1] {ECO:0000313|Proteomes:UP000215289, ECO:0000313|Proteomes:UP000215394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 1038 {ECO:0000313|EMBL:RLM01438.1}, and HMR AF 23
RC {ECO:0000313|EMBL:RHZ71322.1};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequences of two Aspergillus turcosus clinical strains
RT isolated from bronchoalveolar lavage fluid: one azole-susceptible and the
RT other azole-resistant.";
RL Submitted (AUG-2018) 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:RHZ71322.1}.
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DR EMBL; NKHV02000022; RHZ71322.1; -; Genomic_DNA.
DR EMBL; NIDN02000005; RLM01438.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229X2H1; -.
DR STRING; 1245748.A0A229X2H1; -.
DR OrthoDB; 2903547at2759; -.
DR Proteomes; UP000215289; Unassembled WGS sequence.
DR Proteomes; UP000215394; 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; SFLDF00270; L-galactonate_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:UP000215289}.
FT DOMAIN 198..296
FT /note="Mandelate racemase/muconate lactonizing enzyme C-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00922"
SQ SEQUENCE 451 AA; 49944 MW; 7C69D4BEC27656FF CRC64;
MVKITGFTTR DVRFPTSLDK TGSDAMNAAG DYSAAYCILN TDSSYAGHGM TFTIGRGNEI
VCAAISLLAP LVVGKDLDEL TANWGKTWRY LVSDSQLRWI GPEKGVIHLA LGAVVNALWD
LWAKTLNKPV WRIVADMTPE EFVRCIDFRY ITDAITPEEA IALLKEVEPT KQERIKEAEQ
SRAVPAYTTS AGWLGYTEDK LRALLKESVA QGYKHFKLKV GANVEEDRRR LAIAREAIGY
DRGNILMVDA NQVWSVPEAI EWMHQLAEFK PWFIEEPTSP DDILGHAAIK KALENTPHGT
IGVATGEMCQ NRVVFKQLLQ AGALTVLQAD ACRVGGVNEV LAILLLARKF GVPIVPHSGG
VGLPEYTQHL STIDYVVVSG KKSVLEYVDH LHEHFVHPSS VKDGYYVTPM EPGYSVEMKP
ESMDAFAFPG EEGKSWWRTE AAKTILEGPR I
//