ID R9MUD2_9FIRM Unreviewed; 735 AA.
AC R9MUD2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=C818_00835 {ECO:0000313|EMBL:EOS71377.1};
OS Lachnospiraceae bacterium MD308.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235799 {ECO:0000313|EMBL:EOS71377.1, ECO:0000313|Proteomes:UP000014117};
RN [1] {ECO:0000313|EMBL:EOS71377.1, ECO:0000313|Proteomes:UP000014117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-2 {ECO:0000313|EMBL:EOS71377.1,
RC ECO:0000313|Proteomes:UP000014117};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 3-2.";
RL Submitted (APR-2013) 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:EOS71377.1}.
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DR EMBL; ASTE01000010; EOS71377.1; -; Genomic_DNA.
DR AlphaFoldDB; R9MUD2; -.
DR STRING; 1235799.C818_00835; -.
DR PATRIC; fig|1235799.3.peg.892; -.
DR eggNOG; COG3345; Bacteria.
DR HOGENOM; CLU_009640_2_1_9; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000014117; 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:UP000014117}.
FT DOMAIN 29..283
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 649..725
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 477
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 547
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 365..366
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 442
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 475..479
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 525
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 547
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 735 AA; 84274 MW; 23950EEDBC502A3E CRC64;
MAIRYDEERR IFKLDTKHTT YIIGLTPEGY VGHAYYGDYM ESGDVFYLLR TGERPLTPSA
LPREKSSFLD FFPAEYPTGG IGDYRESCLD VRGSAGCRGC EILYDSHRIR KGKPKLNGLP
ASFGTEDETE TLELVCVDKV LNLRVILSYS VFEEEDIITR SVRLINEGEE CLRIEKVLSA
CLDMDDEEFE MVTLVGGWAR ERGVQRRRIT YGKQMVSSAK GESSHQEHPF LALVTPQTTE
QQGRVYAMNF VYSGNFIAEA ELNQHDAVRM VMGINGEDFC WNLRGGEEFQ APEVVLTFSG
EGFGKMSRSF HDFYRKHLIR SPYLHKKRPV LINNWEATYF DFDTEKLLDI AREAKKAGIE
MLVMDDGWFG KRDNDDSSLG DWTVNEDKLK GGLKYLVDEV REIGLEFGIW FEPEMISPDS
MLYREHPEWA IHIPGRQATQ SRAQYVLDLS NPEVVDYAYE CVAKILRSAP ISYVKWDMNR
QLSDLGSSYL ERDSQQELFH RYVLGLYEMQ ERLVSEFPGL LLENCSSGGG RFDPGMLYYS
PQIWCSDNTD AVERLAIQEG TALIYPLSTM GAHVSDCPNH MTGRNTPFET RGHVALAGTF
GYELDITKIP EKDREMIPGQ IKDYHKYNEL IREGDYYRIA SYRENHKYDC YLVAAKDKSE
ALMTFVQVQC VPTFHGKKIK LLGLDSKAVY RLEGTEQVYT GEMLMKGGFI IDFVQGDGMS
RLYHFVRQSE DHIKK
//
