ID A0A0J1J6H7_9FIRM Unreviewed; 729 AA.
AC A0A0J1J6H7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN ORFNames=RHS_1443 {ECO:0000313|EMBL:KLU72746.1};
OS Robinsoniella sp. RHS.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Robinsoniella.
OX NCBI_TaxID=1504536 {ECO:0000313|EMBL:KLU72746.1, ECO:0000313|Proteomes:UP000036477};
RN [1] {ECO:0000313|EMBL:KLU72746.1, ECO:0000313|Proteomes:UP000036477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHS {ECO:0000313|EMBL:KLU72746.1};
RX PubMed=25284151; DOI=10.1016/j.cell.2014.09.008;
RA Seedorf H., Griffin N.W., Ridaura V.K., Reyes A., Cheng J., Rey F.E.,
RA Smith M.I., Simon G.M., Scheffrahn R.H., Woebken D., Spormann A.M.,
RA Van Treuren W., Ursell L.K., Pirrung M., Robbins-Pianka A., Cantarel B.L.,
RA Lombard V., Henrissat B., Knight R., Gordon J.I.;
RT "Bacteria from diverse habitats colonize and compete in the mouse gut.";
RL Cell 159:253-266(2014).
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:KLU72746.1}.
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DR EMBL; JNGB01000013; KLU72746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1J6H7; -.
DR PATRIC; fig|1504536.3.peg.1008; -.
DR Proteomes; UP000036477; 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; 2.60.420.10; 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; 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:UP000036477}.
FT DOMAIN 35..169
FT /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08531"
FT DOMAIN 207..308
FT /note="Alpha-L-rhamnosidase concanavalin-like"
FT /evidence="ECO:0000259|Pfam:PF05592"
FT DOMAIN 312..644
FT /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT /evidence="ECO:0000259|Pfam:PF17389"
FT DOMAIN 648..706
FT /note="Alpha-L-rhamnosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17390"
SQ SEQUENCE 729 AA; 82714 MW; C990D70D603C4569 CRC64;
MEVTFMEWKA KWIKPSLEMG DVCPMFKKKF QTTEKVKKAT LTITSLGVYE ALINGSRVGE
FILAPGWTSY KKRLQYQVYD VTDLLGEENL LLVTVGKGWY RSRMPGWASS KVQSALQQNP
AGLLAQLDIV FEDGSKETIM TNETWTAAES NVRFSEIYDG ETYDASFQSA DETEVCTFDG
PFDTLISQQG EEIREQERVS AACIFTTPCG ETVVDFGQEV TGYIEIEVDA KAGEEVLLSH
AEVMDQDGNF YTENYRSAKA QLHYICKDGH QIYKPKLTFF GFRYIRIDKF PVAVSAAKPE
NFTAVAVHSE MKRTGFLRCS NPLLNKLFDN IIWGQKGNFV DVPTDCPQRD ERLGWTGDAQ
VFIRTACLNY DVEKFFTKWL GDMAADQKED GQVGHVIPNL LDDPDSSAAW ADAATICPWE
LYLAYGNDEI LKSQFNCMKK WIGYITTHTK DEYLWTGGIH FGDWLGLDAP DGSYKGSSRE
DFIASAFYAY STSLVIKAGK VLEEDVAEYE TLYKKILTAF RKTYTEYHTQ TECVLAVYFK
LAPDCQAAAD QLADLVKSCG KQLQTGFVGT PYLLHVLSEY GYTQLAYDLL LRETYPSWLY
PITKGATTIW EHWDGIKENG DFWSKDMNSY NHYAYGSVAD WVYGVAAGIT PLEEYPGYEK
VRIAPMPDQR LDWLEATLET RHGIIRSGWK IEDASWRYEI VTPVAADIVI AGHEYHLEKG
SYLFYSKIK
//
