ID A0A0U3NMX7_9ACTN Unreviewed; 469 AA.
AC A0A0U3NMX7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Beta-xylosidase {ECO:0000313|EMBL:ALV32635.1};
GN ORFNames=AS200_11670 {ECO:0000313|EMBL:ALV32635.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV32635.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV32635.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV32635.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) 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; CP013743; ALV32635.1; -; Genomic_DNA.
DR RefSeq; WP_058922316.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3NMX7; -.
DR STRING; 1725411.AS200_11670; -.
DR KEGG; scx:AS200_11670; -.
DR OrthoDB; 273314at2; -.
DR Proteomes; UP000068029; Chromosome.
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; cd18822; GH43_CtGH43-like; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
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; PTHR22925:SF3; ARABINANASE_LEVANSUCRASE_INVERTASE; 1.
DR PANTHER; PTHR22925; GLYCOSYL HYDROLASE 43 FAMILY MEMBER; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000068029};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..469
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006842532"
FT DOMAIN 338..468
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 469 AA; 50512 MW; F8B26C5E49A75214 CRC64;
MRRAHAVLLA LCLGLFGALA TAGPARAATQ TVTNGTQFTD TSGNPVHAHG GGVIKVGPYY
YWFGEDRNAD NTFRYVDAYR STDLKNWEFR NHVLTQSSAS ELATAYIERP KVVYNASTGK
FVMWMHKENG VDYSQARAAV AVSDTVDGGY TYQGSFQPLG QYMSRDITTF VDTDGTAYMV
SAANENYDLH IYRLTADYTA IDSLVANPWP GGHREAPALF KRGGVYFMLT SGATGWSANQ
QQYATATSLS GPWTSWTNVG DSTAYNSQTA YVLPVTGTSG TSYLYMGDRW GNSFGGTVND
SRYVWLPLTF PTSTSLSLSW YPEVTVDTAA GKVAGTAATY NTLVARNSGK CADVPNQSLW
QGVAISQYTC NGGTNQKWWF KDLGTGYYAL MGRGSSLCLQ ENASTVTQEN CTGAAAQQWS
VVTSGSYATI KARATGECLD VSGASTANSA AIITYTCSGA TNQQWTRGT
//
