ID A0A1R3SVD6_9BACT Unreviewed; 987 AA.
AC A0A1R3SVD6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=PSM36_0104 {ECO:0000313|EMBL:SCD18940.1};
OS Proteiniphilum saccharofermentans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Proteiniphilum.
OX NCBI_TaxID=1642647 {ECO:0000313|EMBL:SCD18940.1, ECO:0000313|Proteomes:UP000187464};
RN [1] {ECO:0000313|EMBL:SCD18940.1, ECO:0000313|Proteomes:UP000187464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3/6 {ECO:0000313|EMBL:SCD18940.1};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) 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; LT605205; SCD18940.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3SVD6; -.
DR STRING; 1642647.PSM36_0104; -.
DR KEGG; psac:PSM36_0104; -.
DR Proteomes; UP000187464; Chromosome i.
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; 3.40.50.880; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 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; IPR035396; Bac_rhamnosid6H.
DR InterPro; IPR035398; Bac_rhamnosid_C.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR029010; ThuA-like.
DR PANTHER; PTHR34987:SF4; ALPHA-L-RHAMNOSIDASE C-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR34987; C, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G02880)-RELATED; 1.
DR Pfam; PF17389; Bac_rhamnosid6H; 1.
DR Pfam; PF17390; Bac_rhamnosid_C; 1.
DR Pfam; PF06283; ThuA; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000313|EMBL:SCD18940.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SCD18940.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000187464}.
FT DOMAIN 48..267
FT /note="ThuA-like"
FT /evidence="ECO:0000259|Pfam:PF06283"
FT DOMAIN 579..904
FT /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT /evidence="ECO:0000259|Pfam:PF17389"
FT DOMAIN 907..977
FT /note="Alpha-L-rhamnosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17390"
SQ SEQUENCE 987 AA; 111959 MW; F0341444228F1D05 CRC64;
MFIFVPEISI PFKIDMKKIL LIALLICSAF QLFADKWDNK TAKLKGKKIL VFTKNGEGFV
HDNIDANVNM FLRLGEQHGF TVDSTSNSTI FSTSDLFQYD AVVFANTNNK VFGNEKEKEG
LVQFNQQGKG IVGIHIACGT EREWDWFKQM IGGTFDFHPR LQKFNVRVVD DKHPSARDIP
SVWNVEDELY IMKEMNPTVR VLMVSDFSSP GFQHSEPMPD TFGTVFPSVW CNEFDGGRQW
VTALGHKKED YSDPLFISHI VGGLQWALAK KESQASIAGK GEWISFDNPQ TVPNTWMIFR
KDIVLDEVPS QLTANIAVDS KYWLWINDRL VVFEGGLKRG PARNATYYDE VEIAPYLTEG
DNTIAVLVWH FGKNSFSHAN SGVCGLFFEA ISPTVEILSD RTWRGGVYDA YEDTGAPFPN
YRLSESNIRF DARKAIKNWN KKIFDGRLSP ASLSGSISDT PLGQLVKRPI PLWKDYGLAA
YPDVRQSGDT LKCTLPYNCH ITPYLKVRAS AGQTIHMLTD NYTGGSANNV RAEYITCEGE
QEYENLGWMN GHEVWYVVPE GIEVLELKYR ETGYDTEFSG RFHCNDEFFN ELWKRSARTL
YVTMRDTYMD CPDRERAQWW GDVVNELGEA FYSLSPSSHQ LALKGIYELM NWQRSDGVIF
SPCPAGNRNQ ELPLQMLASV GWYGFYTQYF YSADSSFVPV VYDRVRRYLH DVWKTDNDGL
VIERPGDWNW GDWGKNVDIG VLTNCWYYLA LKAEQSFALQ MGKTEDARQA AAMMRKIEEN
FDTRFWTGSA YRSPDYKGET DDRSQAMAIV SGLASKSKYP ALLKVLQKEY HASPYMEKYV
LEALFVMNEP EFALERMKKR YSSMLKYAQY TTLFEGWGIG AEGFGGGSIN HAWSGGPLTL
LSQKVCGVEP TSPGFRTFRV APQMGDLTEA EASFESVNGE IKVSVMRSGK RYTIRLTVPE
NSSAEVIFPN GKSVNVSAGD HILHSTN
//