ID A0A1G6TST9_9ACTN Unreviewed; 484 AA.
AC A0A1G6TST9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Beta-xylosidase, GH43 family {ECO:0000313|EMBL:SDD31457.1};
GN ORFNames=SAMN05216270_103102 {ECO:0000313|EMBL:SDD31457.1};
OS Glycomyces harbinensis.
OC Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC Glycomyces.
OX NCBI_TaxID=58114 {ECO:0000313|EMBL:SDD31457.1, ECO:0000313|Proteomes:UP000198949};
RN [1] {ECO:0000313|EMBL:SDD31457.1, ECO:0000313|Proteomes:UP000198949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3516 {ECO:0000313|EMBL:SDD31457.1,
RC ECO:0000313|Proteomes:UP000198949};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; FNAD01000003; SDD31457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6TST9; -.
DR STRING; 58114.SAMN05216270_103102; -.
DR OrthoDB; 177947at2; -.
DR Proteomes; UP000198949; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18820; GH43_LbAraf43-like; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187}.
FT DOMAIN 348..484
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT SITE 158
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 484 AA; 52418 MW; D607F57D0DECD788 CRC64;
MQSIVSVRRI LGLAVALVLV LSMQAFIGAG RAEAAPGPSF TNPVVDVPNS ADPTLVYHAG
FYYYVATTWS SQVVMRKSPT IAGLRAAPEQ VVVSTGGSTM WAPHLEMIDG RWYLYYSVEQ
GSAARRTHVA QSAGSDPMGP YTVRGILDLM PNQGWAIDAA PLRLNGNLYM TFSAFAGDGL
QSLYIAPMTN PWTAGAHGTR ISAPTLSWET QNGAVNEGSF ALQRNGRTFL TYSASHCNGP
NYKIGMLEYT GANPLQMSSW TKAANPLFQR SDANGVYGPG HHSFFTSPDG TETWIAYHAN
DSASDGCGTT RTTRVQRISW NANGTPNLGV PVATTTVLAG PSGEPNLAPV AIRNRHSGLC
LDDYEFGTQP GAEVRQWTCN SETVQDWYLT DLGNGYFAIS NLYSGLCLDD YEFGTQPGAE
VRQWTCNNQN VQQWRITDAG GGYSTIVNRH SGLCLDNYNF GTQPGAEIRQ WTCLNNAAQQ
WTLA
//
