ID A0A1Y4FCZ1_9FIRM Unreviewed; 741 AA.
AC A0A1Y4FCZ1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Alpha-galactosidase {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|PIRNR:PIRNR005536};
DE EC=3.2.1.22 {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|PIRNR:PIRNR005536};
GN ORFNames=B5F53_03265 {ECO:0000313|EMBL:OUO80742.1};
OS Blautia sp. An249.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1965603 {ECO:0000313|EMBL:OUO80742.1, ECO:0000313|Proteomes:UP000195974};
RN [1] {ECO:0000313|Proteomes:UP000195974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An249 {ECO:0000313|Proteomes:UP000195974};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR005536};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase.
CC {ECO:0000256|PIRNR:PIRNR005536}.
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:OUO80742.1}.
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DR EMBL; NFJL01000002; OUO80742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4FCZ1; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000195974; Unassembled WGS sequence.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR CDD; cd14791; GH36; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.70.98.60; alpha-galactosidase from lactobacil brevis; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR038417; Alpga-gal_N_sf.
DR InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR InterPro; IPR002252; Glyco_hydro_36.
DR InterPro; IPR031705; Glyco_hydro_36_C.
DR InterPro; IPR031704; Glyco_hydro_36_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43053:SF3; ALPHA-GALACTOSIDASE C-RELATED; 1.
DR PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 1.
DR Pfam; PF16874; Glyco_hydro_36C; 1.
DR Pfam; PF16875; Glyco_hydro_36N; 1.
DR Pfam; PF02065; Melibiase; 1.
DR PIRSF; PIRSF005536; Agal; 1.
DR PRINTS; PR00743; GLHYDRLASE36.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR005536};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005536};
KW Reference proteome {ECO:0000313|Proteomes:UP000195974}.
FT DOMAIN 29..285
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 651..738
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 480
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 550
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 367..368
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 445
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 478..482
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 528
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 550
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 741 AA; 85678 MW; 167CEC15340EA3D7 CRC64;
MGIYYHQKTK EFHLCNDSVS YIIKVLKNGQ MGQLYFGSRI PDKEDFGYFV ETVHRPMSPC
LFEGDSTYSL EHLKQEYPSY GTTDYREPAF EILQENGSRI SDFVYKSHTI YDGKPELQGL
PAIYTEDTKE AQTLEILLED SVMGAQIVLY YTIMRDYPAI TRSVKIRNYR DSHLRLTKAM
SLCLDLPDRD YEWMQLSGAW ARERHIKTRK LQQGIQAIGS IRGNSSHHHN PFVALKRSSA
DERQGEVIAM SLIYSGNFII QGEVDTYDVT RMLMGIHPTG FTWDLPAGEE FQTPEAVLVY
SENGLNGMSQ TFHKLFRTRL ARGYWRDRER PVLINNWEAT YFDFTEESLL EIAKTAQKAG
VELFVLDDGW FGTRNDDKQG LGDWFANKEK LKEGISGLSR RIEEECQMKF GLWFEPEMVN
ENSQFYRSHP DYRLEAPGRR ASHGRNQHVL DFSRKEVVDS IYQQMEEVLK DAKVSYIKWD
MNRSITECFS RGWPADQQGE IFHRYILGVY DLYERLRKRF PEILFESCAS GGGRFDPGMM
YYAPQAWTSD DTDAVERLKI QYGTSMAYPL SSMGAHISAV PNHQVFRNTP FETRANVAYF
GAFGYELDMN QLSEEEQEEM RRQVAFVKKY RKLIHQGTFY RLLSPFEGNI AAWMVVSEDK
KDAVIGYYKI LNDVNAPYRR VKLQGLDAEG NYAIEGRDGL YSGKELMRAG MITSDPSAGQ
GEEGEPVCSD FWSQIFLLHR V
//
