ID A0A1G4MBP3_LACFM Unreviewed; 494 AA.
AC A0A1G4MBP3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
GN ORFNames=LAFE_0D08350G {ECO:0000313|EMBL:SCW01246.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCW01246.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|EMBL:SCW01246.1, ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6772 {ECO:0000313|EMBL:SCW01246.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58; Evidence={ECO:0000256|ARBA:ARBA00036824};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
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DR EMBL; LT598492; SCW01246.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4MBP3; -.
DR STRING; 4955.A0A1G4MBP3; -.
DR OMA; KSINYEH; -.
DR OrthoDB; 2037007at2759; -.
DR Proteomes; UP000190831; Chromosome d.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF9; GLUCAN 1,3-BETA-GLUCOSIDASE 2; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000190831};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 471..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..346
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
SQ SEQUENCE 494 AA; 55372 MW; A9394A55D47A0AFB CRC64;
MSVHGGYYPT SKIASNWTQA TNWSIQGVTL GGWLVTEPYI TPSLYNQAIE IAGNETGPSI
VDEYTLCSVL SKSTAKDLLS KHYKSWVKES DFKEIKEEGF NLVRIPIGYW AWKKGDDLYD
FGFTNITYED PYVADGLQLA YLNKAMEWSA KYGLKVWLDL HGAPASQNGF DNSGQRNLYG
TPGWLSKEFT GELMFQLLQS VFHSVRDGEY GDNVVGIEVV NEPLGDKIGM EKVEYFYQMT
FQMFEGILGR NESVSMVVHD AFQAAGYWDE YFNPEYSQEL PGNFSYSHTS ASYDSVVVDH
HHYEVFSDGQ LANSRDTRLE DILQYANGLG AEQPYHPAVV GEWSGAITDC ATWVNGVGVG
VRYDGSYYHT TRFNSSLATR PLGKCTSQLP IANWTEEYRV QVREFVEAQL LAYSNATDGW
IFWNWKTESA PEWDYKQLAG AGLFPQPFDN YTFYFANGTR NPGGALPSRN AAHAVGACRA
LVAAAVALVV LYFT
//
