ID A0A1W2BW44_9PSEU Unreviewed; 601 AA.
AC A0A1W2BW44;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glucosylceramidase {ECO:0000313|EMBL:SMC77233.1};
GN ORFNames=SAMN05660733_01574 {ECO:0000313|EMBL:SMC77233.1};
OS Lentzea albidocapillata.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=40571 {ECO:0000313|EMBL:SMC77233.1, ECO:0000313|Proteomes:UP000192840};
RN [1] {ECO:0000313|Proteomes:UP000192840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44073 {ECO:0000313|Proteomes:UP000192840};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family.
CC {ECO:0000256|ARBA:ARBA00005382, ECO:0000256|RuleBase:RU361188}.
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DR EMBL; FWYC01000005; SMC77233.1; -; Genomic_DNA.
DR RefSeq; WP_030479849.1; NZ_JOEA01000018.1.
DR AlphaFoldDB; A0A1W2BW44; -.
DR STRING; 40571.SAMN05660733_01574; -.
DR eggNOG; COG5520; Bacteria.
DR OrthoDB; 9806701at2; -.
DR Proteomes; UP000192840; Unassembled WGS sequence.
DR GO; GO:0004348; F:glucosylceramidase activity; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR033452; GH30_C.
DR InterPro; IPR001139; Glyco_hydro_30.
DR InterPro; IPR033453; Glyco_hydro_30_TIM-barrel.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR11069; GLUCOSYLCERAMIDASE; 1.
DR PANTHER; PTHR11069:SF23; LYSOSOMAL ACID GLUCOSYLCERAMIDASE; 1.
DR Pfam; PF02055; Glyco_hydro_30; 1.
DR Pfam; PF17189; Glyco_hydro_30C; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR PRINTS; PR00843; GLHYDRLASE30.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 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:RU361188};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361188};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..601
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010695217"
FT DOMAIN 477..600
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 601 AA; 63463 MW; 7105C62BF922100F CRC64;
MSKATERWRG IAIAAVVVTA GSTLVSPAAT AATNASVWLT TGDKSNALTK QADVTFGSGG
TGPTITVNPN STHQSMVGFG ASFTDAAAWN IFNSPRRNEI MNNLFDKNNG IGMSFIRQPI
GATDFSRSFY TYNDGAADPS LSRFSIDHDR PYILPLLQQA KQLNPQLAVM ATPWSAPAWM
KNNNNLIRGS LNDSRIGVYA DYLVKFAQAY KAAGIPIDYL SVQNEPLFEP PGYPGMYMSP
QQQVNVINTL VPKLRAAGEQ ARLLGYDHNW DNVDYAQTVN NGAGGNVIGS AWHCYGGNPS
GQSVVKNNQP GKDIFFTECS GTKSANDAAT FRDTLRWQGI NLAIGATRNH ARSVAIWNMA
LDQNNGPVIG SCTNCTGVVT TSGGNVTYNA EYYVLGHLSK FVQPGAVRID STGYGEGGIQ
NVAFRNPNGQ IVLVALNSGG QQNFRVSNGG QTFGYTMPAG AMATFTWPGT LDPGGRTGAI
TGLGGKCLDV TDGSTANGTL PQLWTCFGGP NQTWTLQADG TVRGLGKCLD VTGNGTADGA
AVQLWDCFGG PNQRWTASGG TLVNAGSGKC LDVIGNNTAD GAKLQIWSCT GGANQRWTVP
A
//
