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Database: UniProt
Entry: E8RNG9_ASTEC
LinkDB: E8RNG9_ASTEC
Original site: E8RNG9_ASTEC 
ID   E8RNG9_ASTEC            Unreviewed;      1060 AA.
AC   E8RNG9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   OrderedLocusNames=Astex_0098 {ECO:0000313|EMBL:ADU11800.1};
OS   Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS   NCIMB 9791 / VKM B-1370 / CB 48).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU11800.1, ECO:0000313|Proteomes:UP000001492};
RN   [1] {ECO:0000313|Proteomes:UP000001492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 /
RC   CB 48 {ECO:0000313|Proteomes:UP000001492};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Brun Y.V., Woyke T.;
RT   "Complete sequence of chromosome 1 of Asticcacaulis excentricus CB 48.";
RL   Submitted (DEC-2010) 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; CP002395; ADU11800.1; -; Genomic_DNA.
DR   RefSeq; WP_013477634.1; NC_014816.1.
DR   AlphaFoldDB; E8RNG9; -.
DR   STRING; 573065.Astex_0098; -.
DR   KEGG; aex:Astex_0098; -.
DR   eggNOG; COG3408; Bacteria.
DR   HOGENOM; CLU_002926_3_0_5; -.
DR   Proteomes; UP000001492; Chromosome 1.
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   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; 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:UP000001492}.
FT   DOMAIN          328..496
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          509..607
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          612..953
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          955..1028
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   1060 AA;  117078 MW;  BD3683D951186B0F CRC64;
     MLTRRGALSG AVKGAGLATA ALAVPASAAE KRDGLRLRGL KANLCDNPLG VENQDVRLSW
     QCDSARRGTM QTAWRVEVAS SDAKLRAGLA DLWDSGRVES DQTFDVIYSG KPLTSREKAV
     WRVTAWDCHG RVTTSKPAFW EMALLSPDDW QAEWLAAEDA DMLGDREAGL FWVTADAPSK
     DKSCQVRLVF DLEADAETTV LTISTTSYEV RIDGSLIDLP PRPANAWGPR GVVETVCTLK
     AGTHALTLSL KGEKPQCAML VRARLRDGRV VRFDDLNARA SSEKPEGWTR PDFDASAWPM
     VKRSEREDQP FPGKGAFLMR RDFTATETVA KARLYVTALG AYEAYINGKR VGDALLAPES
     MDFSKRILYR VFDVTKMVGR GENVIGAMVA DGWYGSYTSP QGRFAFGNPP LRFMAQLELT
     YTGGRVERVV TDQSWMISAS PVLSSDIYDG EDYDARREQP GWATPRFQAD ARWSHAAIAP
     PVTGKLQATL SPPIRRLGLL KAKSLKFING SWIVDFGQNF AGFAKIRVKG IAGQKVTLKF
     AEILKPDGSI DQANLRGALA TDTYVLKGDP AGEVWEPRFT YHGFRYVEIS GLSNAPAPDD
     VMGVVIHSDT SRTGHLRIGH PIIQTLWQNS LWSQKSNFMG IPTDCPQRDE RLGWMGDAHV
     FWDAAAFNMD VSAFTQRWMA DVRDAQWPNG AFAFIAPNSM RDTAPNQASP GWADAGVILP
     WTTWQRYGDT DVINQNWEAM SAYIGYVAAL SEDGIWSKGH GWDFGDWLAL DSRWPGDHTT
     PPDLVGTAMW KHSTLAMLDM AKATKRQKAV EDYTRLAEKI DTAFAKAFIH PDATVGNGSQ
     TGYILALRYN LVPPQLRAEV ARKLHDSIVN RGRLLTTGFL GTPHSLDVLA DNGYAALVYD
     LLLRTEYPSW GYMVMKGATT TWERWNGDAG DISMNSFNHY ALGAVIGFVY RRIAGIDPIE
     PGFRRFRFNP ILDRRIGSGG AQYDAVSGRI STDWTLKADG QFKLKLSVPS NTRAEVHLPA
     TNRTDIRENA KPLTLQSLGI VNGRMVIEAG PGDYDFAVMP
//
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