ID S3CVC5_GLAL2 Unreviewed; 383 AA.
AC S3CVC5;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=alpha-galactosidase {ECO:0000256|ARBA:ARBA00012755};
DE EC=3.2.1.22 {ECO:0000256|ARBA:ARBA00012755};
GN ORFNames=GLAREA_03319 {ECO:0000313|EMBL:EPE30352.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE30352.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE30352.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC residues in alpha-D-galactosides, including galactose
CC oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00001255};
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DR EMBL; KE145363; EPE30352.1; -; Genomic_DNA.
DR RefSeq; XP_008081763.1; XM_008083572.1.
DR AlphaFoldDB; S3CVC5; -.
DR GeneID; 19462374; -.
DR KEGG; glz:GLAREA_03319; -.
DR eggNOG; ENOG502SIY3; Eukaryota.
DR HOGENOM; CLU_051214_1_0_1; -.
DR OMA; GCTICES; -.
DR OrthoDB; 1472084at2759; -.
DR Proteomes; UP000016922; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR004352; GH114_TIM-barrel.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR35273; ALPHA-1,4 POLYGALACTOSAMINIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G07890)-RELATED; 1.
DR PANTHER; PTHR35273:SF2; ALPHA-GALACTOSIDASE; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF03537; Glyco_hydro_114; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000313|EMBL:EPE30352.1};
KW Hydrolase {ECO:0000313|EMBL:EPE30352.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 346..383
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 261..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 41117 MW; 371767C8CC10C8D7 CRC64;
MGTSMAADFP VGQKFQIVLN GVPDTGKVLA PADAMVWDVD AEDTTKETIA ALHSLGKTVI
CYFSAGTYEN WRPDAKQFPT GDLGTTLAEW PNEKWIRLSS TGVRNIMKAR IARAAQKGCD
AIDPDNTDAY QNSNGLNMKA TDSIDYIRYI AKYAATLGMK TGLKNSLSII PQVADLMSFA
VNEECAKFSE CDTYNSFIKS GKPVYHIEYV AKPPTITNDE RRIFCTSGGM AGFSTVMKNM
TLNGWTAYCD GSTAITETTP GGIIPGKPPN PHPTSTITTT TSYSWSNTTF TTSTTPTLSE
STVTRTTTTS KSSTTIKTTS RTTSKTSSKT STSKATSSTP APGGGCAQKH WDQCGGNDWK
GCTTCASGFS CKGVSPPYYY QCL
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