ID A0A2K3QH34_9HYPO Unreviewed; 543 AA.
AC A0A2K3QH34;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Alpha-galactosidase {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|RuleBase:RU361168};
DE EC=3.2.1.22 {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|RuleBase:RU361168};
DE AltName: Full=Melibiase {ECO:0000256|RuleBase:RU361168};
GN ORFNames=TCAP_03227 {ECO:0000313|EMBL:PNY26846.1};
OS Tolypocladium capitatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY26846.1, ECO:0000313|Proteomes:UP000236621};
RN [1] {ECO:0000313|EMBL:PNY26846.1, ECO:0000313|Proteomes:UP000236621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY26846.1,
RC ECO:0000313|Proteomes:UP000236621};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes a variety of simple alpha-D-galactoside as well as
CC more complex molecules such as oligosaccharides and polysaccharides.
CC {ECO:0000256|ARBA:ARBA00003969}.
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,
CC ECO:0000256|RuleBase:RU361168};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
CC {ECO:0000256|ARBA:ARBA00009743, ECO:0000256|RuleBase:RU361168}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNY26846.1}.
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DR EMBL; NRSZ01000492; PNY26846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3QH34; -.
DR SMR; A0A2K3QH34; -.
DR STRING; 45235.A0A2K3QH34; -.
DR OrthoDB; 1217107at2759; -.
DR Proteomes; UP000236621; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14792; GH27; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR041233; Melibiase_C.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR11452:SF90; ALPHA-GALACTOSIDASE A-RELATED; 1.
DR PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17801; Melibiase_C; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|RuleBase:RU361168};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361168};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361168};
KW Reference proteome {ECO:0000313|Proteomes:UP000236621};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..543
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014345724"
FT DOMAIN 330..411
FT /note="Alpha galactosidase C-terminal beta sandwich"
FT /evidence="ECO:0000259|Pfam:PF17801"
FT DOMAIN 421..514
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF00652"
SQ SEQUENCE 543 AA; 59149 MW; 0F34607CBE92BFCC CRC64;
MMSAAVLGAV AWLVGTATAG DDTLLPLPPM GFNNWARFMT NINESIFIDA ADAMSKNGLL
AAGYNRLNLD DAWSTKQRAD NGSMVWDPVK FPSGLPWLTD YLKSKGFIPG IYTNAGNLSC
GGYPGALDHE AIDLETFTRW GFKYLKMDGC HLPDKSEATY HEVYGRWYKL LAEAEEPLIL
SDSAPAYFSG QIAGTNNMTD WYKAMGWASA FGQLARHSAD ILVYPDGIFG RGSSWDSMMY
NYGQEVRLAR YQRPGYFNDP DFINADHPSY TLEEKKSHFA LWCSFSAPLI ISANIPTLSQ
DDIKYLTNND LIAIDQDGLI QQATLASSSD TWDVLTKNLE NGDRLLTILN KGSTAGNLSV
PWQRIGLSAK DLSDDVSIKN LWTGEWSNVS VNNGGINATA IPSHGTAVFR IAQTASDVTP
TGIIFNTDST NCLTDNVSGR VTFGKCDGSD GQIWNVWPDG QINSLLRPHN CIVDAQGVIQ
SQESSSHTDT WRYEMSGNLI NSDSGLCLTE GVNGIATASK CGDELNEQVV GLPVGVNVVE
PDS
//
