ID V4NZD2_9CAUL Unreviewed; 548 AA.
AC V4NZD2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:ESQ87087.1};
GN ORFNames=ABAC460_21190 {ECO:0000313|EMBL:ESQ87087.1};
OS Asticcacaulis sp. AC460.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282360 {ECO:0000313|EMBL:ESQ87087.1, ECO:0000313|Proteomes:UP000017839};
RN [1] {ECO:0000313|EMBL:ESQ87087.1, ECO:0000313|Proteomes:UP000017839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC460 {ECO:0000313|EMBL:ESQ87087.1,
RC ECO:0000313|Proteomes:UP000017839};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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 -!- 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:ESQ87087.1}.
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DR EMBL; AWGD01000039; ESQ87087.1; -; Genomic_DNA.
DR RefSeq; WP_023455515.1; NZ_AWGD01000039.1.
DR AlphaFoldDB; V4NZD2; -.
DR STRING; 1282360.ABAC460_21190; -.
DR PATRIC; fig|1282360.3.peg.4128; -.
DR eggNOG; COG3669; Bacteria.
DR OrthoDB; 7176684at2; -.
DR Proteomes; UP000017839; Unassembled WGS sequence.
DR GO; GO:0004560; F:alpha-L-fucosidase activity; IEA:InterPro.
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; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR006311; TAT_signal.
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 SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..548
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004723066"
FT DOMAIN 462..535
FT /note="Alpha-L-fucosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16757"
FT SITE 360
FT /note="May be important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
SQ SEQUENCE 548 AA; 61492 MW; 65D8113786F29EBD CRC64;
MKLSRRNLLT AALPSASLAV AAVSATAANA APAPYKATWE SLGSAYQTPD WFRDAKLGLW
AHWGPQCIPE CGDWYGRQMY IQGNFYYEHH TKTYGHPAQF GFMEFLKDWK AEKFDPDSLL
ALYKSVGAKY FVAMANHHDN FDLYDSKYQA WNAVNIGPKR DICGDFAAAA RKHGLKFGLS
NHAAHAWHWW QTAYGYDAEG PVKGLRYDAA RLTKADGKGR WWDGYDPQEL YTGRFGDMPP
PDGINSIQAM QDHINSTSGQ WLETVPPNGA YYAKKWLLRQ NDMIDKYKPD LVYFDNTGLP
LEQYGLDATA YYYNQAVKWH GTADVIATGK KLDDVQRKAI TEDIERGYSD RLRGNVWQTC
TCIGNWHYDR GLYERNGYKS AKSVIQRLTD IVSKNGNMLL SIPVRGNGEI DEKEVAILGE
MKAWLDVNGE AIFATRPYAI YGEGPFKVVE GHMNEGEAKP FTHEDIRYTT KAGTLYALPL
EWPTSGYVTL ISLAEGSPLR KGTVERVELL GHGQPLKFEL GMDGLTVKLP DARPTFSPAL
KIMGSGLV
//
