ID A0A368VVK7_9BACL Unreviewed; 730 AA.
AC A0A368VVK7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=DFP97_11238 {ECO:0000313|EMBL:RCW44175.1};
OS Paenibacillus prosopidis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=630520 {ECO:0000313|EMBL:RCW44175.1, ECO:0000313|Proteomes:UP000252415};
RN [1] {ECO:0000313|EMBL:RCW44175.1, ECO:0000313|Proteomes:UP000252415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7506 {ECO:0000313|EMBL:RCW44175.1,
RC ECO:0000313|Proteomes:UP000252415};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-2018) 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}.
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:RCW44175.1}.
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DR EMBL; QPJD01000012; RCW44175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368VVK7; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000252415; 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:UP000252415}.
FT DOMAIN 29..286
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 650..726
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 479
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 549
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 367..368
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 444
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 477..481
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 527
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 549
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 730 AA; 82886 MW; AC7A70A34AAD49A2 CRC64;
MSIQYDQQRS LFHLQAQDTS YVIHVTKTGY PAHLYWGKKL RGMQLGRLLE LKERASFSPS
TELDQLALSL DTLPHEYPGY GNSDFRMPAY QVMLPNGTTV TDLRYESHSI RSGKPALAGL
PATYTESDDE AATLELTLKD ELTGLTVILS YTVFEAFNAI TRSARLVNNG TDTLQLLRAF
SLSLDFAHDR FEMLQLSGAW TRERYVHTRK LEPGLQSVES RRGSSSHMQN PFVALLSEGA
NEDHGDVYGV NLVYSGNFTA GVEVDQFHSA RLFMGLNPFD FNWRLEPGEQ FQTPEAVMVH
SGHGLGGMSR SFHDLYRSRL IRGTFRDQTR PILVNNWEAT YFNFNADKIE SIARTGQELG
IELFVLDDGW FGKRDNDTTS LGDWFVDRSK LPNGLEDLVS RVKRLDMQFG LWFEPEMISP
ESELYRAHPD WCLHVEGRRR TQARHQLILD LSRTDVQDYI VKSVSDILSS APITYVKWDM
NRNMTEIGSA LLPPERQRET AHRYMLGLYA VLEKITSAFP QILFESCSGG GGRFDAGMLY
YMPQTWTSDN TDAVSRLKIQ YGTSIVYPVS SMGSHVSAVP NHQVGRITSL ETRGNVALSG
NFGYELDLTR FTDEEKETVK AQVALYKDVR HLVQFGDFYR LLSPFEGNDT AWMFVSKDQS
EAFVVYASVL QEPNPPLNRF RLKGLDAKRD YRLDEQGTVY GGDELMYAGL ATPQFHGDYA
SKVYRFRAVE
//
