ID Q9RJU1_STRCO Unreviewed; 1085 AA.
AC Q9RJU1;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN OrderedLocusNames=SCO0369 {ECO:0000313|EMBL:CAB55731.1};
GN ORFNames=SCF41.28c {ECO:0000313|EMBL:CAB55731.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB55731.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAB55731.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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; AL939105; CAB55731.1; -; Genomic_DNA.
DR RefSeq; NP_624692.1; NC_003888.3.
DR RefSeq; WP_011027059.1; NZ_VNID01000015.1.
DR AlphaFoldDB; Q9RJU1; -.
DR STRING; 100226.gene:17757952; -.
DR CAZy; GH78; Glycoside Hydrolase Family 78.
DR PaxDb; 100226-SCO0369; -.
DR PATRIC; fig|100226.15.peg.345; -.
DR eggNOG; COG3387; Bacteria.
DR HOGENOM; CLU_002926_1_1_11; -.
DR InParanoid; Q9RJU1; -.
DR OrthoDB; 9761045at2; -.
DR PhylomeDB; Q9RJU1; -.
DR Proteomes; UP000001973; 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; IPR008979; Galactose-bd-like_sf.
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; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001973};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..1085
FT /note="alpha-L-rhamnosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030176914"
FT DOMAIN 360..537
FT /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08531"
FT DOMAIN 548..643
FT /note="Alpha-L-rhamnosidase concanavalin-like"
FT /evidence="ECO:0000259|Pfam:PF05592"
FT DOMAIN 651..976
FT /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT /evidence="ECO:0000259|Pfam:PF17389"
FT DOMAIN 979..1050
FT /note="Alpha-L-rhamnosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17390"
SQ SEQUENCE 1085 AA; 117277 MW; 537FD7B13A8D5AC3 CRC64;
MPRTNPPVRH RTAAALAGVT AFVTLLAGAV TADAATTGTI TPTALRTQHL TEALGIDDTT
PDLSWQTTAG APNTRQAAYR VQAATSLQRL RASRPDLWDS GKVESSVPGT TYAGKDPGSR
AKVYWRVMLW SGKGKRHSGW STTAVFETGL TRQSDWDAQW ITHPDWRLSD RTVEPVVVHL
PRTTARYVRL DVTRLGLPLA ESFPGRTWRL QVGEIDVRDS TTATTGLARG AAVTASESNT
VRKSWEPALA VDGLPNSALQ TAAGYASAAH TGPDVSDAPI TLTLDLKSVK TFDEVALYPR
ADVLTDDGRI PGLPVDYTVS AADSADGPAT RLAAVTGQRQ PTPYLPAGLP LLTDDFTLPK
RVRSARLYIA GLGVYDATVN GEPVGDAVLE PANTDFAERV QYATYDVTDR LRTGANTLGV
ALGNGMSNVV STADRYRKLY GNLSDPKLIA RLEVTLADGR VRTITSGDDW RTTLGPTTAS
NWYGGEDYDA RREIPRWDEP AGDRRGWRHA VAVAGPGTAD RPALLSARET EPIRVVETLK
GKEVDGAEGS RVFDLGRNIA GWPEITVRAP EGTAIRVYPA ESLKDGHAFQ SISNVGAPLW
DSYTTAGGWH AESWHPRFSY HGFRYLELRG VPENATVSVR GHVLRTDNAS AGDFTSSDPL
INGIHSLIRR SIEGNMMSVL TDCPSREKLG WLEQNQLVFP ALAGNYDMRA YLRKIVRDMA
DAQTPDGLVP STVPEYTSLP GAYRNDSNWG GAFVLVPWQL YLTYGDRQTL ETYYPDMRRY
AAFLEAQAAD GILDYGLGDW FTPDRTFPRA VAGTYGYWRV VDTLGRIASL LGDTAAADEY
RRKAAASVEA LTAKYYDATT GTFGGGGHGA EALALDMGAY PQGERDRLLS HFTDAIKDAG
NHLVLGEISL PAAFRVLSAA DRDDVVHAIA TQTTSPSYGY QVLAGNTTLG ESWDGGPGQS
QNHFMLGAID SWFTTRVAGI SQTEDSVGYA KLLVDPAVEG DMTSAAGSYR TPYGVARTDW
ERSDDRFRLT VDVPAGSTAE VHVPVAGEHA EAPGSARLLR LTGGEAVYEV GSGHWTFRST
MERGR
//
