ID A0A3R7M2M0_PENVA Unreviewed; 452 AA.
AC A0A3R7M2M0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=alpha-L-fucosidase {ECO:0000256|ARBA:ARBA00012662};
DE EC=3.2.1.51 {ECO:0000256|ARBA:ARBA00012662};
GN ORFNames=C7M84_010472 {ECO:0000313|EMBL:ROT71220.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT71220.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT71220.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT71220.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT71220.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT71220.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-
CC 1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the
CC carbohydrate moieties of glycoproteins.
CC {ECO:0000256|ARBA:ARBA00004071}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:0) + H2O = a
CC neolactoside nLc4Cer(d18:0) + L-fucose; Xref=Rhea:RHEA:49308,
CC ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:91119,
CC ChEBI:CHEBI:91121; Evidence={ECO:0000256|ARBA:ARBA00000419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49309;
CC Evidence={ECO:0000256|ARBA:ARBA00000419};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:1(4E)) + H2O = a
CC neolactoside nLc4Cer(d18:1(4E)) + L-fucose; Xref=Rhea:RHEA:48224,
CC ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:17006,
CC ChEBI:CHEBI:28691; Evidence={ECO:0000256|ARBA:ARBA00000321};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48225;
CC Evidence={ECO:0000256|ARBA:ARBA00000321};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 29 family.
CC {ECO:0000256|ARBA:ARBA00007951, ECO:0000256|PIRNR:PIRNR001092}.
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:ROT71220.1}.
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DR EMBL; QCYY01002329; ROT71220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7M2M0; -.
DR STRING; 6689.A0A3R7M2M0; -.
DR EnsemblMetazoa; XM_027364330.1; XP_027220131.1; LOC113812444.
DR Proteomes; UP000283509; Unassembled WGS sequence.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006004; P:fucose metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR016286; FUC_metazoa-typ.
DR InterPro; IPR031919; Fucosidase_C.
DR InterPro; IPR000933; Glyco_hydro_29.
DR InterPro; IPR018526; Glyco_hydro_29_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10030; ALPHA-L-FUCOSIDASE; 1.
DR PANTHER; PTHR10030:SF46; ALPHA-L-FUCOSIDASE-RELATED; 1.
DR Pfam; PF01120; Alpha_L_fucos; 1.
DR Pfam; PF16757; Fucosidase_C; 1.
DR PIRSF; PIRSF001092; Alpha-L-fucosidase; 1.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00385; ALPHA_L_FUCOSIDASE; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001092};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001092};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 361..446
FT /note="Alpha-L-fucosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16757"
FT SITE 279
FT /note="May be important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
SQ SEQUENCE 452 AA; 52073 MW; 553FD6C41BCCB2E7 CRC64;
MLRTLQQQDS DFGLAGAKYE PTWDSLDSRP LPAWYDAAKV GIFIHWGVFS VPSFGSEWFW
KYWHDGKGKY VEFMERNYRP GFTYADFAPE FTAEFFEPEE WASVFNASGA RYVVLTSKHH
EGFTLWPSRY SWNWNSLDVG PKRDLVGDLA QAIRTKTPHI HFGLYHSKYE WFNAMYLEDK
ARGFETQDFV KAKTLPELYE LVNTYEPEIV WSDGDWEAPD SYWDSTHFLA WLFNESPVKD
NVVVNDRWGK GVVCNHGSYY TCSDRYNPGT LQHHKWENCL TLDKVSWGFR REAPLRDYLT
IQELLATLAE TISCGGNLLV NIGPTHDGHL PAIMEERLRQ LGSWLDVNGQ AVYESTPWTH
QSDAVTPGVW YTAKGDDVYA FVLRWPEDGA VTLGSVLPTS RTKAYMLGHV EKVKPLQFTK
TEKGQLTVML PLMHQVRGQW AWVLLLSDVM AA
//
