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Database: UniProt
Entry: A0A261EQU9_9BIFI
LinkDB: A0A261EQU9_9BIFI
Original site: A0A261EQU9_9BIFI 
ID   A0A261EQU9_9BIFI        Unreviewed;       944 AA.
AC   A0A261EQU9;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=BOCO_1038 {ECO:0000313|EMBL:OZG49229.1};
OS   Bombiscardovia coagulans.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bombiscardovia.
OX   NCBI_TaxID=686666 {ECO:0000313|EMBL:OZG49229.1, ECO:0000313|Proteomes:UP000216004};
RN   [1] {ECO:0000313|EMBL:OZG49229.1, ECO:0000313|Proteomes:UP000216004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22924 {ECO:0000313|EMBL:OZG49229.1,
RC   ECO:0000313|Proteomes:UP000216004};
RX   PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA   Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA   Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA   van Sinderen D., Ventura M.;
RT   "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT   family.";
RL   BMC Genomics 18:568-568(2017).
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};
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:OZG49229.1}.
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DR   EMBL; MWWS01000005; OZG49229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261EQU9; -.
DR   OrthoDB; 9761045at2; -.
DR   Proteomes; UP000216004; Unassembled WGS sequence.
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; 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; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216004}.
FT   DOMAIN          146..272
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          316..412
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          420..760
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          765..839
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   944 AA;  104350 MW;  83F1086BF19CC189 CRC64;
     MTDILVSKVR FGQHRVSDRV LGYASARPAL SWEISSAPKG WKQTTVQIEV SQDAEPAERY
     TVYTSNQICV PWPSKPLQSR EARAVRIRVA GTDGAWSPWS QRSCVETGLL HNEDWQGSPV
     TTDRTIGREN PAPIMSRTFT VGQECNLARL DITAGGIFVP YIDGQRVGSD QLAPGWTDYK
     QRFNALTYDV TELLSAGEHE LAVVLGNGWY RGQLTWNCRT NVYGSQLWLL ANVRWQDQNG
     SHSIATNEDW TWRPSSILEN DSYDGQTQDM RIPLLNPHGK RGGVIPLPMP SARIRPQEAP
     TAQVIRQLPG QKLIITPSGK RIVDFGQNLS GWVRMHIHAG HAGQEVVLKH AEVLEHGELG
     TRPLRKAKAT DRFILSDQEE YIEPMFTQHG FRYVQVDGID DFSVDDLQAC LVSAAMEPLA
     SFISSEADLN RLFHNARWST MDNFLTVPTD CPQRDERLGW TGDIAMFAPT ALSLFDAGSF
     LSSWLVDMSN SQSSDGGIPV VVPDVLDGPK LTCGWGDAAV LVPMAVYQAT GDTEVLRRFL
     PMMDKFIDGV DAQCGHSHLW RGGFQFGDWL DPDAPADNPG GSKADPDVVA TAYFAHSARL
     VASAHAVLNQ KTHAHRYAQL ADEIAVAFRQ EYVTDMGNIL SDCESVYAMA LVWGLLETPQ
     QKKGAAERLA DIVRVSGFRI ATGFLGTPLV CEALTLSGYS HLAIRLLLQK RCPSWLYPVS
     MGATTIWERW DSMLPDGSIN PGEMTSFNHY ALGAIVHWIL DGLAGLHMKE PAWRKVRISP
     VIDAALPHIA VKQKTPYGQI ALDWTLGDDS FDLNLDLPVG IEAEIALPGE EDRIYTHGHH
     SWKLPRSKVC KPQGSIQSIR DLIDSQEHLE ALEQALLSSR SPLYQGNQAD VTFTKAAKPW
     LDADLAALPD VASQQGYVPK ADDIVESVKG FLSAQSSSKE NQHQ
//
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