ID A0A077EBZ2_9FLAO Unreviewed; 459 AA.
AC A0A077EBZ2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Alpha-L-fucosidase {ECO:0000313|EMBL:AIL44992.1};
GN ORFNames=BD94_1217 {ECO:0000313|EMBL:AIL44992.1};
OS Elizabethkingia anophelis NUHP1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=1338011 {ECO:0000313|EMBL:AIL44992.1, ECO:0000313|Proteomes:UP000028933};
RN [1] {ECO:0000313|EMBL:AIL44992.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL44992.1};
RX PubMed=24012265; DOI=10.1016/S0140-6736(13)61858-9;
RA Teo J., Tan S.Y., Tay M., Ding Y., Kjelleberg S., Givskov M., Lin R.T.,
RA Yang L.;
RT "First case of E anophelis outbreak in an intensive-care unit.";
RL Lancet 382:855-856(2013).
RN [2] {ECO:0000313|EMBL:AIL44992.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL44992.1};
RX PubMed=26019164; DOI=10.1093/gbe/evv101;
RA Li Y., Liu Y., Chew S.C., Tay M., Salido M.M., Teo J., Lauro F.M.,
RA Givskov M., Yang L.;
RT "Complete Genome Sequence and Transcriptomic Analysis of the Novel Pathogen
RT Elizabethkingia anophelis in Response to Oxidative Stress.";
RL Genome Biol. Evol. 7:1676-1685(2015).
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}.
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DR EMBL; CP007547; AIL44992.1; -; Genomic_DNA.
DR RefSeq; WP_024565138.1; NZ_CP007547.1.
DR AlphaFoldDB; A0A077EBZ2; -.
DR STRING; 1338011.BD94_1217; -.
DR KEGG; eao:BD94_1217; -.
DR eggNOG; COG3669; Bacteria.
DR HOGENOM; CLU_002934_0_3_10; -.
DR Proteomes; UP000028933; Chromosome.
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; IPR000933; Glyco_hydro_29.
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 PIRSF; PIRSF001092; Alpha-L-fucosidase; 1.
DR PRINTS; PR00741; GLHYDRLASE29.
DR SMART; SM00812; Alpha_L_fucos; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..459
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001718231"
FT SITE 302
FT /note="May be important for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR001092-1"
SQ SEQUENCE 459 AA; 53296 MW; A08EBF59E9E4F3D5 CRC64;
MKKIFLSLLL CSSLGAFAQG YIPPKEPEVQ QKLKQWQDKK FGIIIHWGLY SIPGIVESWN
LCSEEEDWIP RPKNINYDDY KKWYWGLSKQ FNPIKFNPEA WAKMAKDAGM QYVVFSTKHH
DGFNMFDTKQ TDFKITNPEV PFSKNPKSNI AKEVFNAFRK EGLWVGAYFS KPDWHSENYW
WPYYATYNRN NNYSIDKNPE RWDAFKKYTY NQLEELASQY GKLDLFWLDG GWVRPSNPEK
YKGDKSYKGS QDIDMDKIAG MLRGYQKDLI IVDRSVHGIY ENYTTPEREI PEKPLNYPWE
ACDPLGDNWG YVPNDPMKST NKVIHTLAEI ISKGGNYLLG IGPDGNGEFD PRVNKTLKEI
GNWMKTNAEA VYGTKPIAPY ADGNFRFTQK GNSVYAFYLV PENNTQLPQN LQFSFPKKFK
KVSVLGSNKA VKFEQQANNM NISTSDIKQQ PHAVVFKME
//