ID A0A089LD78_9BACL Unreviewed; 766 AA.
AC A0A089LD78;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=R50912_23945 {ECO:0000313|EMBL:AIQ42754.1};
OS Paenibacillus sp. FSL R5-0912.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536771 {ECO:0000313|EMBL:AIQ42754.1, ECO:0000313|Proteomes:UP000029512};
RN [1] {ECO:0000313|EMBL:AIQ42754.1, ECO:0000313|Proteomes:UP000029512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-0912 {ECO:0000313|EMBL:AIQ42754.1,
RC ECO:0000313|Proteomes:UP000029512};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) 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; CP009282; AIQ42754.1; -; Genomic_DNA.
DR RefSeq; WP_042238175.1; NZ_CP009282.1.
DR AlphaFoldDB; A0A089LD78; -.
DR KEGG; paeq:R50912_23945; -.
DR HOGENOM; CLU_009640_2_1_9; -.
DR Proteomes; UP000029512; 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:UP000029512}.
FT DOMAIN 28..287
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 652..759
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 766 AA; 85262 MW; F1D4E7AE47025F7B CRC64;
MNIYADETLG LFHLQSKDTS YIIQLVEGYP AHVYWGPQLR HDNSLTGALE LRERASFSPT
PLLQKPTLSL DALPQEYPQY GTSDFRRPAY QVQLADGTRI SELQYAGYAI TPGKPVLEGL
PAVYVENEAE AQSLELTLKD DYAGLSVKLM YTVFADHSAI TRSVRFEHNG EAPLRLEQAL
SASVDFADSS YDTLHLSGAW ARERHVQRRP LTPGAALSLE SRRGSSSHQT NPFLALLRPG
ADEDQGDVFG FNLVYSGSFA ATAEVEQFGQ TRVSIGINPF DFSWLLEPGQ SFQTPEAVLV
YSSEGLGGMS RTYHRLYRTR LCRGVHRDQA RPILVNNWEA TYFDFDADKI AAIAKEAGPL
GIELFVLDDG WFGTRDRDNS SLGDWFEDRR KLPEGLADLA SRVNSEGLQF GLWVEPEMVS
PDSDLYRKHP DWCLHAAGRR RTEGRNQLIL DLSRPEVCDY LYETLSAVFS SAPITYVKWD
MNRNMTEIAS AKASPERQKE TAHRYMLGLY HLLERLTSRF PHILFESCSG GGGRFDPGIL
FYMPQTWTSD NTDAIERLAI QYGTSMVYPA SSMGAHVSAV PNHQVDRITS LATRGDVAMS
GNFGYEMDLT KFTEAEKDLA ARQIAQYKEI RTLVQQGDMY RLLSPFEGSG DTAWMFVSED
KTEAFVAYFR VLAIPNAPIS RLTLKGLHPE LDYVIETGAK GSIAHVHGGA EASAPAEGDS
SAPFQTAFDG TPLGGDRLMQ IGLVVSDLRG DYASCTYRLR AVQRQS
//
