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Database: UniProt
Entry: L0FX23_ECHVK
LinkDB: L0FX23_ECHVK
Original site: L0FX23_ECHVK 
ID   L0FX23_ECHVK            Unreviewed;       944 AA.
AC   L0FX23;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   OrderedLocusNames=Echvi_0927 {ECO:0000313|EMBL:AGA77200.1};
OS   Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Echinicola.
OX   NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA77200.1, ECO:0000313|Proteomes:UP000010796};
RN   [1] {ECO:0000313|Proteomes:UP000010796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC   {ECO:0000313|Proteomes:UP000010796};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Echinicola vietnamensis DSM 17526.";
RL   Submitted (FEB-2012) 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; CP003346; AGA77200.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0FX23; -.
DR   STRING; 926556.Echvi_0927; -.
DR   KEGG; evi:Echvi_0927; -.
DR   PATRIC; fig|926556.3.peg.948; -.
DR   eggNOG; COG3408; Bacteria.
DR   HOGENOM; CLU_002926_1_1_10; -.
DR   Proteomes; UP000010796; 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; IPR013783; Ig-like_fold.
DR   InterPro; IPR008902; Rhamnosid_concanavalin.
DR   PANTHER; PTHR33307:SF11; ALPHA-L-RHAMNOSIDASE; 1.
DR   PANTHER; PTHR33307; ALPHA-RHAMNOSIDASE (EUROFUNG); 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010796}.
FT   DOMAIN          209..376
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          389..472
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          499..832
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          835..908
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   944 AA;  106691 MW;  CF53BDC6A0B1CC92 CRC64;
     MKVEKNYTEP LALMQAWLFL LIAVVLFSGC DSGPRGTLLQ VTNITTELAD NPMNIEKTAP
     RFGWELVSDA NGARQTAYQV VVSHSASEDE AAVVWDSGKI TSGQSQLIPY EGGPLINGER
     YFWKVKVWNE AGISSDWSNM AFFEMAPYEL EKGAQWIGAI TRAESGLPAG RNYHEPDMRR
     EENKEKWSKV KPLAKRSIQL RKPFEVESEI EKATVYISGL GHYELKLNGE KVGNSEFAPL
     WSDYDKTVYY NAYDVTERLV SGENAIGVLL GNGMYNVSGD RYAKFLISFG PPTLFFHLKI
     TYADGEEQLI SSDDSWKWSE SPITFNCVFG GEDYDATLEQ DGWAQPGFDD RNWKPVVIQE
     APKGKLCPQH ASPVLVQKQY DIKATAEPEE NTYVLDMGQN LAGFPSIKVK GQKGQKVKLV
     VGEHLKESGL VGQGRTGGPH YYEYTLKGDE EESWQPRFSF YGYQYIQVTD VNVPGQEQQA
     DRPTITEIKS NFIYNDATEE GTFESSNEIF NQTHLLINNA IKSNMQSVFT DCPHREKLGW
     LEETHLNGPG LFYNYDLTQL VPKVMQDMAD AQRENGLVPN IAPEYVVFGG DFTDSPEWGV
     ASVVLPWMYY DYYGDSSLIQ EYYPMMKKYI DYLGTTADNH IVSHGLGDWY DYGEHAAGYS
     KNSPIALSAT SHYYFGVKLL KKAALMLQKG VDYREYSRLE KQVKEAFNQT FFDPETNQYG
     TGSQFSNAVP LFLDMVDSTK REAVLAHLVQ DIEAHGYRLT TGDVGNRYLY QTLARNGLNE
     VMFKMHNHYD TPGYGFQIKF GLTTLTEQWD PRKGNSWNHF MMGQIEEWFY RDLAGIQPDP
     DQPGFKHFLL KPQWVGDMTF VKASYESIYG TIASSWKKEE GNAQFHFDIP ANTSATLVLP
     VEQSAEVRIN GSRTEKAKGV SKVQADGHPS FELGSGKYSI EVKF
//
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