ID A0A087D3G2_9BIFI Unreviewed; 739 AA.
AC A0A087D3G2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=BSCA_0399 {ECO:0000313|EMBL:KFI90062.1};
OS Bifidobacterium scardovii.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=158787 {ECO:0000313|EMBL:KFI90062.1, ECO:0000313|Proteomes:UP000029033};
RN [1] {ECO:0000313|EMBL:KFI90062.1, ECO:0000313|Proteomes:UP000029033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21589 {ECO:0000313|EMBL:KFI90062.1,
RC ECO:0000313|Proteomes:UP000029033};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFI90062.1}.
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DR EMBL; JGZO01000034; KFI90062.1; -; Genomic_DNA.
DR RefSeq; WP_046726034.1; NZ_JGZO01000034.1.
DR AlphaFoldDB; A0A087D3G2; -.
DR STRING; 158787.BSCA_0399; -.
DR GeneID; 85166834; -.
DR eggNOG; COG3345; Bacteria.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000029033; 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; 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.
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:UP000029033}.
FT DOMAIN 35..291
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 655..734
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 484
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 554
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 372..373
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 449
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 482..486
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 532
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 554
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 739 AA; 82193 MW; C64361A8EBC479B9 CRC64;
MDDHMQRSLV RVNDELRQFH LSNGRISMIL GVAAGKLVNL YTGAAVPDSA DFGYLHDDRF
RVQSSTVDER TERFVEQQRL EYPEFGRGDY RHPAIEVAQP NGSRLTDLQY VGYSVSPGKP
ALAGLPATFA GGGSVATTLD IVLCDELIGL AVTLRYTIFR DDPVIARSAL IENRGMEPLT
LERAASFNLD LPDADYTMTE FTGAWARERT PRTQPLHPGI QQIESLRGAS GPYFSPNAIF
ARPATTEDEG EAFGLAFVYS GNFDLHAEVD TYGATRLQLG INPLGFAWRL EPGESFQTPE
ALLGYTDRGL NTLSQSFHRA VLDHLQRPQW ARRERPILIN NWEATYFDFT EDKLLDLARL
AKRVGIELFV LDDGWFGART SDNAGLGDWT ANPDRLPEGI AGIARKINDL GMDFGLWFEP
EMVNKDSDLY RAHPDWVLST PGRGQSVYRN QYVLNFANPA VVDGIFGQMH AILSGANVAY
IKWDMNRFIT EAFDATRGAE RQGEVMHRYM LGVYALYERL FAAFPDLIIE GCASGGSRFD
LGVLAYSPQI WTSDDTDAIE RLSIQYGTSY FFPVSAMGAH VSITPNHQTG RSTSLDMRAA
VAMFGTFGYE MDLTSLPDAE LEAIAGQVAF FKEHAPLLHN GDLYRLIAPY GHRRAAWMSV
SADRAHAIVG DYVILGQPNR GKSRLYLRGL DAEARYHAVS TDGRFEATRS GGEFMRIGID
DSDLGPDFAS RIYLVDRVD
//
