ID A0A1I5Y266_9BACT Unreviewed; 672 AA.
AC A0A1I5Y266;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Alpha-galactosidase {ECO:0000256|RuleBase:RU361168};
DE EC=3.2.1.22 {ECO:0000256|RuleBase:RU361168};
DE AltName: Full=Melibiase {ECO:0000256|RuleBase:RU361168};
GN ORFNames=SAMN05444277_110106 {ECO:0000313|EMBL:SFQ38351.1};
OS Parafilimonas terrae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Parafilimonas.
OX NCBI_TaxID=1465490 {ECO:0000313|EMBL:SFQ38351.1, ECO:0000313|Proteomes:UP000199031};
RN [1] {ECO:0000313|EMBL:SFQ38351.1, ECO:0000313|Proteomes:UP000199031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28286 {ECO:0000313|EMBL:SFQ38351.1,
RC ECO:0000313|Proteomes:UP000199031};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|RuleBase:RU361168};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
CC {ECO:0000256|ARBA:ARBA00009743, ECO:0000256|RuleBase:RU361168}.
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DR EMBL; FOXQ01000010; SFQ38351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5Y266; -.
DR STRING; 1465490.SAMN05444277_110106; -.
DR Proteomes; UP000199031; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14792; GH27; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.120.1060; NPCBM/NEW2 domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013222; Glyco_hyd_98_carb-bd.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041233; Melibiase_C.
DR InterPro; IPR038637; NPCBM_sf.
DR PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE; 1.
DR PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR Pfam; PF05345; He_PIG; 1.
DR Pfam; PF16499; Melibiase_2; 2.
DR Pfam; PF17801; Melibiase_C; 1.
DR Pfam; PF08305; NPCBM; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SMART; SM00776; NPCBM; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49313; Cadherin-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|RuleBase:RU361168};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361168};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361168};
KW Reference proteome {ECO:0000313|Proteomes:UP000199031};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..672
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011619099"
FT DOMAIN 26..166
FT /note="Glycosyl hydrolase family 98 putative carbohydrate-
FT binding module"
FT /evidence="ECO:0000259|SMART:SM00776"
SQ SEQUENCE 672 AA; 74118 MW; 44F0C11099C5049F CRC64;
MKRKINALRI MLLVVACTLW CAVGSAQNNI ARLDALDIKS FSEGIPGIVT KTNAGGGPLK
IGGHYFSSGI GTNGVSVLPF LLDGDAISFT AGVGPDDEAN PLSTYKFYVI GDKKILFESK
DMKVGDQPEK IQVNLSGIQR LGLLVMVDAA NLSRSYSDWV DAAFVMKPGY MPEHIPNTGE
KYILTPASSA LPKINSAKVF GATAGNPFLF AVAATGVRPM YFTASNLPQG LNIDSATGII
SGKVNNKGIY PVVLKAKNKW GETTNILKIK IGDTIALTPP IGWNGWNSWA REIDKDKVLA
SAHAMVSKGL HNHGWTYINI DDAWQGRREG SDKALQPNEK FPGFKDMADS IHALGLKLGV
YSTPWITSYA GYAGGSSNFE DGSYPDSVRD NKRQYRYTGK YRFENADARQ MAAWGVDYLK
YDWRIDVQSA QRMQEALRKS GRDIVFSISN SAPFDSAATW KKTANVWRTG PDIRDSWTSL
YYSAFLLDKW APYAGPGHWN DADMLIVGNV TTGSKMHPTR LTPDEQYSHV SIFSLLNLPL
LIGCPIDQLD AFTLNLLTND EVIEIDQDPL GKPARLIIED KGVQVWVKPM EDGSYAVGLF
NLAGFGKTPQ SFFRWGDEKP VSYQFDFSKA GLLGKWKLRN VWKQQDMGIF SNQFKTVIPH
HGVVLLRMYK AG
//
