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Database: UniProt
Entry: A0A0P0NK23_9SPHI
LinkDB: A0A0P0NK23_9SPHI
Original site: A0A0P0NK23_9SPHI 
ID   A0A0P0NK23_9SPHI        Unreviewed;       894 AA.
AC   A0A0P0NK23;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=AQ505_22005 {ECO:0000313|EMBL:ALL07926.1};
OS   Pedobacter sp. PACM 27299.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1727164 {ECO:0000313|EMBL:ALL07926.1, ECO:0000313|Proteomes:UP000062859};
RN   [1] {ECO:0000313|EMBL:ALL07926.1, ECO:0000313|Proteomes:UP000062859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 27299 {ECO:0000313|EMBL:ALL07926.1,
RC   ECO:0000313|Proteomes:UP000062859};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-rhamnose residues
CC         in alpha-L-rhamnosides.; EC=3.2.1.40;
CC         Evidence={ECO:0000256|ARBA:ARBA00001445};
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DR   EMBL; CP012996; ALL07926.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P0NK23; -.
DR   STRING; 1727164.AQ505_22005; -.
DR   KEGG; pep:AQ505_22005; -.
DR   OrthoDB; 9766741at2; -.
DR   Proteomes; UP000062859; Chromosome.
DR   GO; GO:0030596; F:alpha-L-rhamnosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR016007; Alpha_rhamnosid.
DR   InterPro; IPR035396; Bac_rhamnosid6H.
DR   InterPro; IPR035398; Bac_rhamnosid_C.
DR   InterPro; IPR013737; Bac_rhamnosid_N.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008902; Rhamnosid_concanavalin.
DR   PANTHER; PTHR33307; ALPHA-RHAMNOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR33307:SF6; ALPHA-RHAMNOSIDASE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF05592; Bac_rhamnosid; 1.
DR   Pfam; PF17389; Bac_rhamnosid6H; 1.
DR   Pfam; PF17390; Bac_rhamnosid_C; 1.
DR   Pfam; PF08531; Bac_rhamnosid_N; 1.
DR   PIRSF; PIRSF010631; A-rhamnsds; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062859};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..894
FT                   /note="alpha-L-rhamnosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006052173"
FT   DOMAIN          173..344
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          354..464
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          470..795
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          804..871
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   894 AA;  100928 MW;  3C9D15932C845867 CRC64;
     MIPNINKRIY GCLFLFFSLS SFPSFSQQQI HAEQLQCEHM ISPIGIDALQ PRLAWKLKDD
     RRAAVQSAYR ITVSTDSLAL MKKEGSRVWD SGKIGSSAQL TNYSGKGLDP FTKYYWQVQI
     WDKDGKPAAF IPISSFETGM LKMSNWKGTW ISDNKDINKL PAPYFRKEFK ADKKIKSARA
     YMAAAGLYEL YLNGEKVGNH RLDPMYTRFD RRNLYVSYDV TAQLKNGENA VGVLLGNGWY
     NHQSLAVWDF DKAPWRARPT FCLDLRITYT DGSTDVVLSD DSWKTDDSPI VFNSIYTAEH
     YDARKEQKGW NTAGFDDRKW KGIALRAAPS KQIVSQVMHP IRNVEEIPVK SVRKFNDTTY
     VFDLGRNIAG VSEIKLKGDR GTRLSIKHGE RLLANGRLDL SNIDVYYRPK DQNDPFQTDI
     FILNGQGTEA FMAKFNYKGF QYIEVTSSKP INLNNESIIG HFMHSDVPVA GKIHTSSEMV
     NKLWAATNNS YLSNLFGYPT DCPQREKNGW TGDGHFAVET GLYNFDGITV YEKWLADHQD
     EQQPNGVLPD IIPTGGWGYG KSNGTDWTST IAIIPWNIYL FYGDPHLLRS CYPNIKSYVD
     YVTQISPDGL TTWGRGDWVP VKSESPLEYT SSVYYFTDAI ILAKAAKLFG KVEDYKHYSA
     LAEKIKKAIN DKYLNRNEGI YGTGLQTELS VALLWGIVPE DLRIKVAQKL ADRVKADNMH
     LDVGVLGAKA ILNALSENGQ ADIAYKLAVQ DTYPSWGWWI ANGATTLYEN WNIQAGRDIS
     LNHMMFGEIG GWFFKGLGGI MTDEKAPGFK NIRLMPHFVT GLNEFESIHE GPFGTIQSSW
     KRNGQKIIYE VHIPANSSAT IHFPLEAGQS ARMAGTMLPE VYQASAGKYT FEIQ
//
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