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Database: UniProt
Entry: A0A1C7IHX3_9FIRM
LinkDB: A0A1C7IHX3_9FIRM
Original site: A0A1C7IHX3_9FIRM 
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
//
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