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Database: UniProt
Entry: A6EG28_9SPHI
LinkDB: A6EG28_9SPHI
Original site: A6EG28_9SPHI 
ID   A6EG28_9SPHI            Unreviewed;       901 AA.
AC   A6EG28;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   ORFNames=PBAL39_07240 {ECO:0000313|EMBL:EDM35462.1};
OS   Pedobacter sp. BAL39.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=391596 {ECO:0000313|EMBL:EDM35462.1, ECO:0000313|Proteomes:UP000003664};
RN   [1] {ECO:0000313|EMBL:EDM35462.1, ECO:0000313|Proteomes:UP000003664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL39 {ECO:0000313|EMBL:EDM35462.1,
RC   ECO:0000313|Proteomes:UP000003664};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) 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};
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:EDM35462.1}.
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DR   EMBL; ABCM01000013; EDM35462.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6EG28; -.
DR   STRING; 391596.PBAL39_07240; -.
DR   eggNOG; COG3387; Bacteria.
DR   Proteomes; UP000003664; 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:UP000003664};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..901
FT                   /note="alpha-L-rhamnosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002695095"
FT   DOMAIN          179..350
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          360..470
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          475..801
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          805..881
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   901 AA;  100500 MW;  559230FAC87A95D6 CRC64;
     MNHKKETYMK DHLKNSFYAC CLLTLTGASL LSSAYAQQPV ALQCEHLVRP LGVDAAHPRL
     SWMMDDKSQG AAQRAYRITV DTDSMAVLKG QGGTWDSGKT SSGLSLTTYQ GKALQPFTKY
     YWKVELWDKD GQPAASKQIS SFETGMMGME NWKGDWISDS EDINALPAPY FRKAFATSKK
     IKSARAYVAA AGLYELYLNG KKVGDHRLDP MYTRFDRRNL YVTYDVTTQL QKGQNAVGVL
     LGNGWYNHQS IAVWNFDKAP WRGRPTFCLN IRITYDDGTT ALVTSGKDWK TDASPITLNS
     IYTAEHYDAR LEQKGWNTAG FNDSKWKAVM KRTAPSKNVT TQLMHPIRNV QTLDVKSVKK
     FNDTTYLFDL GQNISGVTKI KVKGPNGTVL RIKHGERLYP NGRLDLSNID VYYRPKDKND
     PFATDIFTLA GNGLEEFMPK FNYKGFQYVE VSSSQPVTLT KESLTGYFMH SDVPATGNLD
     SSNPLINKLW WATNNSYLSN LMGYPTDCPQ REKNGWTGDG HFAIETGLYN FDGITVYEKW
     LADHRDEQKP NGVLPDIIPT GGWGYGTANG TDWTSTIAII PWNIYLFYGD SKLLADCYDN
     IKKYVGYVES ISPEGLTTFG RGDWVPVKSP SSLEYTSSIY YYVDATILAK AAHLFGKEAD
     VKYYTALAAK IKNAVNKKYF NAETGIYASG VQTELSMPLQ WGVVPDGMEN KVAENLARRV
     VADNMHLDVG VLGAKAVLNA LSENGQADIA YRLAAQDTYP SWGWWIVNGA TTLYENWNIQ
     AERDISLNHM MFGEIGGWFF KGLGGIKPDE QQPGFKNVLL NPNFVTGLDH FEASHDGPYG
     KITSSWKRTG NGISYSVIIP ANATATLNLP VKEGQKVRQE GQELAAKGIL LTAGKHTFEL
     N
//
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