ID A0A1V2M729_9FIRM Unreviewed; 738 AA.
AC A0A1V2M729;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=AN641_01245 {ECO:0000313|EMBL:ONI43835.1};
OS Epulopiscium sp. SCG-C07WGA-EpuloA2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Candidatus Epulonipiscium.
OX NCBI_TaxID=1712378 {ECO:0000313|EMBL:ONI43835.1, ECO:0000313|Proteomes:UP000189533};
RN [1] {ECO:0000313|Proteomes:UP000189533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ngugi D.K., Miyake S., Stingl U.;
RL Submitted (AUG-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|ARBA:ARBA00001255,
CC ECO:0000256|PIRNR:PIRNR005536};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase.
CC {ECO:0000256|PIRNR:PIRNR005536}.
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:ONI43835.1}.
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DR EMBL; LJHE01000078; ONI43835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2M729; -.
DR STRING; 1712378.AN641_01245; -.
DR Proteomes; UP000189533; 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:UP000189533}.
FT DOMAIN 26..280
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 641..734
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 473
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"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 361..362
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 438
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 471..475
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 521
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 543
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 738 AA; 84342 MW; 53183669A757EF9D CRC64;
MILFNNGTFH IYNNDISYII KILRNNHLGQ LYFGKAIKHR DNFDHLLVEK ATVLAPCVFQ
GDLDFSLEIL KQEYPCYGTG DYRDPAYQIT SDNGSSITDL VYKSHVIRQG KSSIEGLPST
YGDNVETLEI TLRDDLIGLE VTLKYHIFDN ISSIIRSAEF SNIGDKVLKI NRAMSSCLDL
YDSNFEMLTL DGAWARERHI TTRKIKSGIQ AISSSRGASS AMHNPFIALK RPNTTEHVGD
VYGFSLIYSG NFLAQVEVDA FDVTRVIIGI NPFEFNWSLQ PNKKFHAPEA VLVYSDKGLN
GMSQNFHNLF KNNLMRGKYK GKSRPILINN WEATYFDFTE ESILKIAKTA KQAGIELFVL
DDGWFGKRDN DSTSLGDWSV YLKKLPNGIK GLAEKINALK LDFGLWFEPE MVNEISELYK
THPDYVISTP NRNRSYGRNQ YVLDFSRTEV VNYIFNKMCE TLDTANISYI KWDMNRNITE
AYSYSLAETQ QKEFFHRYIL GVYSLYEKLT NKFPNILFES CASGGARFDP GMLYYAPQAW
TSDDTDAIER LHIQYGTSMV YPIVSMGSHV AAVPNHQVNR VTSLKMRADV AYFGTFGYEL
DLNKVSPEEL EQVKKQINFF KKYKEVIQLG DFYRLQNGNY YSWIVVSPDK KTAILGYYKI
LAAPNPSFKK INLVGLNENF KYTCNNKTYY GDELMNFGLV LETEFTGSLQ SDSFKGKYTP
GTDKGDFTSQ IYVFEANI
//
