ID K4R291_STRDJ Unreviewed; 654 AA.
AC K4R291;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Alpha-glucuronidase {ECO:0000313|EMBL:CCK26789.1};
DE EC=3.2.1.139 {ECO:0000313|EMBL:CCK26789.1};
GN Name=aguA1 {ECO:0000313|EMBL:CCK26789.1};
GN ORFNames=BN159_2410 {ECO:0000313|EMBL:CCK26789.1};
OS Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK26789.1, ECO:0000313|Proteomes:UP000008043};
RN [1] {ECO:0000313|EMBL:CCK26789.1, ECO:0000313|Proteomes:UP000008043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC {ECO:0000313|Proteomes:UP000008043};
RX PubMed=23043000; DOI=10.1128/JB.01592-12;
RA Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA Pelzer S., Kalinowski J., Mack M.;
RT "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT heterologous production of the unique antibiotic roseoflavin.";
RL J. Bacteriol. 194:6818-6827(2012).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE971709; CCK26789.1; -; Genomic_DNA.
DR RefSeq; WP_015657183.1; NC_020504.1.
DR AlphaFoldDB; K4R291; -.
DR STRING; 1214101.BN159_2410; -.
DR KEGG; sdv:BN159_2410; -.
DR PATRIC; fig|1214101.3.peg.2446; -.
DR eggNOG; COG3661; Bacteria.
DR HOGENOM; CLU_007125_1_0_11; -.
DR OrthoDB; 339499at2; -.
DR Proteomes; UP000008043; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0046559; F:alpha-glucuronidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045493; P:xylan catabolic process; IEA:InterPro.
DR Gene3D; 3.90.1330.10; Alpha-glucuronidase, C-terminal domain; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR037054; A-glucoronidase_C_sf.
DR InterPro; IPR011099; Glyco_hydro_67_C.
DR InterPro; IPR011100; Glyco_hydro_67_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR39207; ALPHA-GLUCURONIDASE A; 1.
DR PANTHER; PTHR39207:SF1; ALPHA-GLUCURONIDASE A; 1.
DR Pfam; PF07477; Glyco_hydro_67C; 1.
DR Pfam; PF07488; Glyco_hydro_67M; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000313|EMBL:CCK26789.1};
KW Hydrolase {ECO:0000313|EMBL:CCK26789.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008043}.
FT DOMAIN 120..405
FT /note="Glycosyl hydrolase family 67 catalytic"
FT /evidence="ECO:0000259|Pfam:PF07488"
FT DOMAIN 431..651
FT /note="Glycosyl hydrolase family 67 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF07477"
SQ SEQUENCE 654 AA; 71799 MW; C9DE5D57E7FB3646 CRC64;
MPLPVPVLPD GVDPAWLPPA AFEAIGRRRT LIRGSGLLVD TVHGEVAEAC ARFGGSVVRD
ASPEPCDLVL DVSGTDDGEA FTLKRAEGRT TVTASGRHGL LHGLFHLVRL GEEAFRGERA
AHTHRPAVAL RVLDHWDNVA VHPVMGQVER GYSGGSLFWR DGRARGDLER VRVYARLLAA
CGINAVTVNN VNVHATEARL LTERIGDVAR IAEAFRPYGI RTHLSVSFAA PILLGGLDTA
DPLDHGVRRW WERATAEVYA AIPDFGGYLV KADSEGQPGP FAYGRSHADG ANLLAAALAP
YGGTVRWRAF VYDHRQDWRD RSTDRARAAY DHFVPLDGEF AANAVLQVKH GPMDFQVREP
VSPLLGAMPG TRLAVEMQAT QEYTGQQRHA CWLGPMWSEA LRFRPEGTDP VGGLSDGLVA
VSNAGADPFW TGHPLAQSNL YTFGRLAWDP GADPLAILDD WIGLTFGPDP AEGVRAVLAG
SWRTYEKYTA PLGVGFMVQP GHHYGPSVDG YEYSPWGTYH FADRDGIGVD RSVATGTGYA
GQYAKPWAEV YESPASCPDE LLLFFHHVPY GHVLHSGKTV IQHIYDTHFE GVEEVEEARE
VWGSLGQSVD PERHARVTER FAEQLRCARE WRDQINSYFL RKSGVPDERG RALY
//
