ID A0A1T2XND2_9BACL Unreviewed; 729 AA.
AC A0A1T2XND2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BVG16_02430 {ECO:0000313|EMBL:OPA81203.1};
OS Paenibacillus selenitireducens.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1324314 {ECO:0000313|EMBL:OPA81203.1, ECO:0000313|Proteomes:UP000190188};
RN [1] {ECO:0000313|EMBL:OPA81203.1, ECO:0000313|Proteomes:UP000190188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES3-24 {ECO:0000313|EMBL:OPA81203.1,
RC ECO:0000313|Proteomes:UP000190188};
RA Xu D., Yao R., Zheng S.;
RT "Genome analysis of Paenibacillus selenitrireducens ES3-24.";
RL Submitted (JAN-2017) 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:OPA81203.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MSZX01000001; OPA81203.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T2XND2; -.
DR STRING; 1324314.BVG16_02430; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000190188; 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:UP000190188}.
FT DOMAIN 28..286
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 649..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 729 AA; 82986 MW; 0D45CD5F84847007 CRC64;
MTIYYDEAKQ LFHLQSKDTS YVIQIVKGFP SHVYWGKKLR ADSNLDGIIT PTERASFSPT
PFPEDKRLSL DTLPQEFPQY GTSDFRDPAY QVQLRDGSRI SELSYLSHRI VEGKPSLDGL
PAVYTESQDE AQTLELDLID SHSGMTVTLS YTVFRDHNAI TRSAKFYNPS SESIQVWRAL
SASIDLSDAS YEAIYLSGAW ARERHVQRRP LGPGATRIES RRGSSSHQQN PFLALVRPET
NEHQGDVYAF NLVYSGSFVA SAEVDQFATT RVNIGINPFD FGWNLEPGAS FQTPEAVLVY
SDEGLGGMSR TFHRLYRTRL CRGVHRDVER PILVNNWEAT YFNFNADKIE AIAKSASQLG
IELFVLDDGW FGKRDDDTTS LGDWFEDRKK LPEGLHNLAQ RVNETGVQFG LWFEPEMVSP
ESELYREHPD WCLHVPNRRR TEGRNQLILD MSRTDVREYL YKRLSTIFST VPISYIKWDM
NRNMTEIGSA DRPAVQQTET VHRYMLGLYE LLERLTSDFP NILFESCSGG GGRFDPGMLY
YMPQTWTSDD TDAIERLKIQ YGTSMVYPVS TMGAHISAVP NHQVERMTSL TMRGDVAMSG
NFGYELDLTR FTEEENEIAK QQISFYKEIR GLVQQGDLYR IKSPFEGNET AWMFVSEDHS
EALVFYFNVL AEPNGPLRRL ALRGLDADKN YRVDASGEVF GGDRLMHVGL DVSSVRGDFT
SKVFKLSAV
//
