ID R7J858_9BACT Unreviewed; 734 AA.
AC R7J858;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=BN646_01039 {ECO:0000313|EMBL:CDE59921.1};
OS Parabacteroides sp. CAG:409.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides; environmental samples.
OX NCBI_TaxID=1262913 {ECO:0000313|EMBL:CDE59921.1, ECO:0000313|Proteomes:UP000018199};
RN [1] {ECO:0000313|EMBL:CDE59921.1, ECO:0000313|Proteomes:UP000018199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:409 {ECO:0000313|Proteomes:UP000018199};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE59921.1}.
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DR EMBL; CBJG010000111; CDE59921.1; -; Genomic_DNA.
DR AlphaFoldDB; R7J858; -.
DR STRING; 1262913.BN646_01039; -.
DR Proteomes; UP000018199; 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:UP000018199}.
FT DOMAIN 45..282
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 641..729
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 546
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 361..362
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 441
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 524
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 546
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 734 AA; 84231 MW; 7DADE1101C4ADA06 CRC64;
MKKYLILFIL LISGWHIAVR AESTGEVIRI STDETDLIYR QAPNGRLYQV YLGPKLMHQT
DLEHFSPFAK GGSDGSAGQR GWEIYMTSGA EDFFEPALGI THADGNMSTI LTYVSSEQKA
IDSNATETII RLKDNQYPLQ VVMHYVAYKK ENVIKTWTEI SHQEKKPIRL NRYASSIIYF
ERPSYYLTEF NGDWAKEMNM TTQQLQYGKK ILDTKLGTRA AMHVYPFFEL GFGQPAEEHR
GEVVLGTIGW TGNFRFTFEV DNVGNLRVIS GINPYASHYE LKAGETFTTP EFIFTRSDEG
KGDASRSFHQ WARNYQLYDG KGDRLTLLNN WENTYFNFDQ DKLSTLMVEA KSLGVNLFLL
DDGWFGNEFP RNDDHAGLGD WQVMKSKLPD GIPFLVKEAK KAGVKFGIWI EPEMVNPKSN
LAQKHPDWII RLPNRETYYY RNQLVLDLTN PEVQDFVFDV VDNLLTENPE IAFFKWDCNS
PITNIYSPYL KDKQEQLYVD YVRGLYKVLD RIRAKYPAVP MMLCSGGGAR CDYGALKYFT
EFWASDNTDP VERLFIQWGF SQFFPSKAIC AHVTSWNKNT SVKFRVDVAM MCKMGFDIGL
KDLNADELTF CQEAVANYHR LKPIILNGDF YRLVSPYDTE HMAVMHVGDN QKKAILYAYD
IHPRYAESTY PVLLQGLDPA KMYMVEEINL MPDTESGAAI NGQTYSGDYL MKVGVRVFSA
RQTTSHIFEI TALD
//
