ID G2NBA8_STREK Unreviewed; 1065 AA.
AC G2NBA8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
DE Flags: Precursor;
GN ORFNames=SACTE_0366 {ECO:0000313|EMBL:AEN08309.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN08309.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN08309.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN08309.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(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};
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DR EMBL; CP002993; AEN08309.1; -; Genomic_DNA.
DR RefSeq; WP_014044301.1; NC_015953.1.
DR AlphaFoldDB; G2NBA8; -.
DR STRING; 862751.SACTE_0366; -.
DR KEGG; ssx:SACTE_0366; -.
DR PATRIC; fig|862751.12.peg.398; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002926_3_0_11; -.
DR OrthoDB; 9761045at2; -.
DR Proteomes; UP000001397; 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; 3.
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 InterPro; IPR006311; TAT_signal.
DR NCBIfam; NF041573; rhamnosid_Stmyc; 1.
DR PANTHER; PTHR33307:SF10; 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.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001397};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1065
FT /note="alpha-L-rhamnosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003433943"
FT DOMAIN 348..510
FT /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08531"
FT DOMAIN 528..626
FT /note="Alpha-L-rhamnosidase concanavalin-like"
FT /evidence="ECO:0000259|Pfam:PF05592"
FT DOMAIN 632..963
FT /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT /evidence="ECO:0000259|Pfam:PF17389"
FT DOMAIN 965..1037
FT /note="Alpha-L-rhamnosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17390"
SQ SEQUENCE 1065 AA; 114395 MW; 3B59F3D0D5309294 CRC64;
MISRRRLLST TAATAALAAV SSPAARAAAP ADTAAGRLRV TGPTVEYVRR PLGLDVSRPR
LSWPLASDHP DHGQSAYQVR VATSPDRLAR PDVWDSGKVV SPTSVLVPYA GPALVSRTRY
HWSVRVWDQD GRVSAWSEPS WWETGLLDEA DWSAGWIGAP AALTSSPSLE AASWIWFPEG
DPAVGAPAAT RWFRGRVEIP EGVTRARLVM TADDGFTALV DGVQVARTEP DGPAENWRRP
VVVDVTAHLS PGSRVVAVTA TNAVDGPAGL LGALELTTAD GAVTLATGTG WRATDREPDG
DWASGGYDDT GWPAAAVLAP WGSGPWGEVR AALSPATQLR TEFRLGRKRV ARARLYSTAL
GLYEVFLNGA RVGEDRLAPG WTDYRKRVQY QTYDVTALLR SGGNALGVTL APGWYAGNIA
WFGPHQYGER PAVLAQLEVT FTDGSIERVL SGTGWAAATG PVTATDLMAG EEYDARLETD
GWSRAGFDAS GWLAAEAVEG VTAVPVAAVD GACRVERELT AREVTEPEPG VYVFDLGQNM
VGTVRLLVSG PAGTTVRLRH AEVLNPDGTL YTANLRTARA TDTYTLRGGG PETYEPRFTF
HGFRYVEVTG FPGRPGPDAV VGRVIHTSAP FTMAFSTDVP MLDRLHSNIT WGQRGNFLSV
PTDTPARDER LGWTGDINVF APTAAYTMES ARFLGKWLQD LRDDQLADGA FPNVAPDLPG
VGSGAAGWGD AGVTVPWALY QAYGDVRVLE QSWSSMVAWL EYLQAHSDGL LRPADGYGDW
LNIEDETPKD VIGTAYFAHS ADLTARTAEV LGKDPGPYRT LSGRVRDAFR AAYVGDGGRV
KGDTQTAYVL ALSMDLLEPG DRAPAADRLV ALIEAKDWHL STGFLGTPRL LPVLTDTGHT
DVAYRLLTRR TFPSWGYQID RGATTMWERW DSVRPDGGFQ DAGMNSFNHY AYGSVGEWMY
ANIAGIAPAA PGFREIRVRP RPGGGVHRAE ARFDSLYGPV TTRWTSDGGG FALRVVLPAN
TTAEVWVPGG DGRSSVRGTA VFLRREDGCA VFAAGSGIHR FTAPA
//
