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Database: UniProt
Entry: A0A3L9DU61_9STRE
LinkDB: A0A3L9DU61_9STRE
Original site: A0A3L9DU61_9STRE 
ID   A0A3L9DU61_9STRE        Unreviewed;       721 AA.
AC   A0A3L9DU61;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, 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=EAF07_04345 {ECO:0000313|EMBL:RLY03768.1};
OS   Streptococcus hillyeri.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=2282420 {ECO:0000313|EMBL:RLY03768.1, ECO:0000313|Proteomes:UP000279194};
RN   [1] {ECO:0000313|EMBL:RLY03768.1, ECO:0000313|Proteomes:UP000279194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=28462 {ECO:0000313|EMBL:RLY03768.1,
RC   ECO:0000313|Proteomes:UP000279194};
RA   Macfadyen A.C., Waller A., Paterson G.K.;
RT   "Streptococcus hillyeri sp. nov., isolated from equine tracheal sample.";
RL   Submitted (OCT-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:RLY03768.1}.
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DR   EMBL; RCVM01000006; RLY03768.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L9DU61; -.
DR   OrthoDB; 9758822at2; -.
DR   Proteomes; UP000279194; 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:UP000279194}.
FT   DOMAIN          29..281
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   DOMAIN          642..718
FT                   /note="Glycosyl hydrolase family 36 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16874"
FT   ACT_SITE        474
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   ACT_SITE        543
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
SQ   SEQUENCE   721 AA;  82298 MW;  9656B28E307C8072 CRC64;
     MIEYKECKRL FHLKTREFSY VIQILENNLL INRYFGKKIK YFSDDNKIAY QDRAFSPNPT
     SKDRTFSLDT LPLEFSSNGL GDFRTSAIEV SNEYGTALDL KYKSHRIYQG KDYLKGLPAS
     FGNEDVVETL EIELYDSLSD VTVVLSYSVF EERNVITRSA KVIAGKTAIH LEKLLSFTLD
     FPHKDFDVHT LTGRYGYEKE WTKTPLTQGK YSIGSIRGAS SHSRTPFIAL ASPEATEQSG
     EIYSAHLIYS GNFTAFAETT AIHTTRLGMG LNDEKFRWVL EPGQEFQSPE AILSYTDKGF
     TGMTRDSHEF IRHHLTRGTF AQKERPILIN NWEGTYFDFT EDKLISLASE AAKVGIELFV
     LDDGWFGKRN SDTCSLGDWV ENREKLPNGL KGLAKKVNDL GMTFGLWFEP EMVSEDSDLY
     REHPNWAIQI TGRGHTYSRE QLVLDLSQDE VCDYIIESVS NVLNSANIGY VKWDMNRNIT
     NIPENQANHE KHEFYHRYIL GLYRILETLN QRFPNVLFES CSGGGGRNDL GMLYYMPQAW
     ASDNTDAIGR LSIQEGTSLI YPTISMGSHV SAVPNHQVGR ITPLETRGNV AMLGNLGYEL
     DLTQLESSEL EEIAEQVETY KSIRQTVQFG DYYRLQKTDN TYAYNLISKD KSQVVFTFVK
     ILSQPEAPFI RVRLEGLDPE ATYYCEKLSA SFGGDELMNI GLTIPYVQKD YFSLQYIFNK
     K
//
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