ID A0A172TH71_9BACL Unreviewed; 729 AA.
AC A0A172TH71;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=SY83_08070 {ECO:0000313|EMBL:ANE46234.1};
OS Paenibacillus swuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1178515 {ECO:0000313|EMBL:ANE46234.1, ECO:0000313|Proteomes:UP000076927};
RN [1] {ECO:0000313|EMBL:ANE46234.1, ECO:0000313|Proteomes:UP000076927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY6 {ECO:0000313|EMBL:ANE46234.1,
RC ECO:0000313|Proteomes:UP000076927};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Paenibacillus swuensis/DY6/whole genome sequencing.";
RL Submitted (JAN-2015) 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 36 family.
CC {ECO:0000256|ARBA:ARBA00006202}.
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DR EMBL; CP011388; ANE46234.1; -; Genomic_DNA.
DR RefSeq; WP_068605769.1; NZ_CP011388.1.
DR AlphaFoldDB; A0A172TH71; -.
DR STRING; 1178515.SY83_08070; -.
DR KEGG; pswu:SY83_08070; -.
DR PATRIC; fig|1178515.4.peg.1603; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000076927; 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 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:UP000076927}.
FT DOMAIN 29..285
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 648..725
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 478
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 548
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 366..367
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 443
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 476..480
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 548
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 729 AA; 82988 MW; 70AACE032B6FC4AA CRC64;
MGILINEQQL TFHLQSRGTS YILQIHEMGF LTHLYWGRRL QAFQPEQLLT YAQRCSFHPT
PDKSKLMTLD TLPQEYPVYG TSDFRQPAYG VKLANGTTIT ELLYVSHTVS AGKPELEVLP
ATYVEDESEA ETLEITTLDK LTGLKVILSY TVFSELDAIT RSVRFVNEGT DNLELQRALS
ANVDFPHKDF DLLHLAGAWA KERNVAKRPL TVGTQSIESR RGSSSHQHNP FLALMSKDAG
EEQGDVYGFS LVYSGNFLAS VEVDAYDTAR VSMGINPFDF SWLLEPGQSF QTPEAVLVYS
PEGLGGMSRR FHKLYRTRLC RGLYRDEVRP VLVNNWEATY FNFNAEKIED IAKAGKELGI
ELFVLDDGWF GKRDSDNSSL GDWIVDRKKL PNGLEDLVKR VRDMEMQFGL WFEPEMVSPD
SDLYRAHPDW CLHVPGRRRT EGRQQLILDF SRKDVCDYII KSLSDVLSSA PITYVKWDMN
RNMTEIGSAL LPAQRQRETA HRYMLGLYRV LEEITTKFPH ILFESCSGGG GRFDPGMLYY
MPQTWTSDNT DAISRLKIQY GTSMVYPISS MGSHVSAVPN HQVHRMTSLD MRGNVAMSGN
FGYELDLTQF TEEEKSTVKA QVAFYKEVRS LVQQGDFYRL LSPFEGNETA WMFVSEDQRD
VFAAYFRVLA EPNDAIRRLR FKGLDPNHSY KVAETGQVYG GDVLMYAGLV LPELHGDYQS
AVWRLQAVE
//
