ID A0A1C7IHX3_9FIRM Unreviewed; 763 AA.
AC A0A1C7IHX3;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-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=A4V09_19485 {ECO:0000313|EMBL:ANU77732.1};
OS Blautia pseudococcoides.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1796616 {ECO:0000313|EMBL:ANU77732.1, ECO:0000313|Proteomes:UP000092574};
RN [1] {ECO:0000313|Proteomes:UP000092574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL58 {ECO:0000313|Proteomes:UP000092574};
RA Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA McCoy K.D., Macpherson A.J.;
RT "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT Diverse Mouse Microbiota 2 (sDMDMm2).";
RL Submitted (APR-2016) 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}.
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DR EMBL; CP015405; ANU77732.1; -; Genomic_DNA.
DR RefSeq; WP_065543838.1; NZ_CP065312.1.
DR AlphaFoldDB; A0A1C7IHX3; -.
DR SMR; A0A1C7IHX3; -.
DR STRING; 1796616.A4V09_19485; -.
DR KEGG; byl:A4V09_19485; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000092574; Chromosome.
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-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:UP000092574}.
FT DOMAIN 29..287
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 651..758
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 368..369
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 763 AA; 87916 MW; 4A5504D5DAB469E2 CRC64;
MAVIFHEKTK EFHIFNREVS YLMRIMENGQ LENLYYGKVI RDKEDFGYLH EEAMRSQMSV
CIPEPGILSM QYTRQEYPVY GTGDYRSPAL TVLQENGSRL VDFSYVSHEI YKGKKGIPPL
PSTYAESEDE AETLEVTLHD QVTDTDLVLT YTIYEDYPVI TRNARFEQKG EQKIVLERAM
SASVEFLDMD YELVQLSGAW SRERYVKNRK LEMGIQSVHS LNGTCGGAEH NPFIALKRPQ
TTENQGEVYG FSLVYSGNFL AQAEVSTFDM TRVMLGINPE DFSWELNQGE SFQTPEVVMV
YSDRGLNKMS QAYHRLYRTR LMRVTWRDKA RPILLNNWEA TYFDFNEEKI LKIAEKAKEA
GVELFVLDDG WFGARNDDYR GLGDWYVNLE KLPDGIAGLS RKVEALGLKF GLWVELEMVN
KDSDLYRAHP DWLIGAPDRF ESHARHQHVL DFSRKEVVDY IYKMIAKVLR ESSISYIKWD
MNRYMTEPYS RGADASQQGK VMHKYILGVY DLYTRLTTEF PEILFESCAS GGARFDPAML
YFAPQTWTSD DTDASERTKI QYGTSYVYPV VSMGSHVSAV PNHQMHRMTP IETRANVAYF
GTFGYELDLN LLSEAELESV KKQIAFMKEY RELIQVDGDF YRLLSPFEGN ETAWMVVAQD
KSRAVAAFYQ RMNKVNASWI RFKLQGLDAG TLYEVSCDMA PSASYDESLA KIYGIQTEEN
MVKTYRAYGD ELMQVGIPID REDLNKKGGD FASLLYTLKK VTD
//