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Database: UniProt
Entry: A0A371ASZ0_9FIRM
LinkDB: A0A371ASZ0_9FIRM
Original site: A0A371ASZ0_9FIRM 
ID   A0A371ASZ0_9FIRM        Unreviewed;       712 AA.
AC   A0A371ASZ0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
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=DWV06_14790 {ECO:0000313|EMBL:RDU22669.1};
OS   Anaerosacchariphilus polymeriproducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerosacchariphilus.
OX   NCBI_TaxID=1812858 {ECO:0000313|EMBL:RDU22669.1, ECO:0000313|Proteomes:UP000255036};
RN   [1] {ECO:0000313|EMBL:RDU22669.1, ECO:0000313|Proteomes:UP000255036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCWD5 {ECO:0000313|EMBL:RDU22669.1,
RC   ECO:0000313|Proteomes:UP000255036};
RA   Kim W., Yang S.-H., Oh J., Lee J.-H., Kwon K.K.;
RT   "Anaerosacharophilus polymeroproducens gen. nov. sp. nov., an anaerobic
RT   bacterium isolated from salt field.";
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.
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:RDU22669.1}.
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DR   EMBL; QRCT01000049; RDU22669.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A371ASZ0; -.
DR   OrthoDB; 9758822at2; -.
DR   Proteomes; UP000255036; 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:UP000255036}.
FT   DOMAIN          10..266
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   DOMAIN          631..705
FT                   /note="Glycosyl hydrolase family 36 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16874"
FT   ACT_SITE        459
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   ACT_SITE        529
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
SQ   SEQUENCE   712 AA;  82006 MW;  57C2E79164EF2896 CRC64;
     MYQMCVDKLG YLLHLYYGST IENEDLDYLI RYIDRACSGQ PYDALDDRTY SLDILPQEYS
     TFGSGDYRTS SILVENSDGS QTVDLRFKEF TIYEGKYKLQ GLPSVYAKEE ADTLEIILED
     KHTNMEVVLL YGVFKNLDVI TRAVRVKNNG AESVYLNRVL STCLDFYENK YDFISFYGKH
     MLERQLERRH LTHGKTSVES VRGVSSHHQN PFVILCDRKA DEDIGDCYGF SFVYSGNFLA
     ETEVDQINQT RFVMGINPTG FRYCLKSQEE FIAPEVVMVF SQNGLGELSR IYHDVYRDHL
     CRGNYAKKQR PVLINNWEAT YFDFDEQKIL DIASMAADVG IEMLVMDDGW FGKRNNDLAG
     LGDWVVNHDK IPSGINGLCQ KINDLGIKMG LWFEPEMVNE DSDLYRAHPD WCIKVPERSP
     VRARYQLVLD VSRKEVRDYI FDLITKVLDG TNIEYIKWDM NRNLTDLYSA GLSKESQGEL
     FHRYVLGVYD LMERLIQRYP NILLENCSGG GGRFDPGMLY YSPQIWCSDN TDAIDRIKIQ
     YGTSFGYPIS SMGAHVSVTP NHGNGRCTDF KTRGIVAMAG TFGYELDITK LSDEEKDMIQ
     SQIEEFKRNY DVIQYGDYYR LTDVMNNHDF AAWQFVDKQK TKSLCSYVSL TAKANAPTVR
     LRLKGLDASK KYRINKEDKI YSGDLLMKAG FVVPETFGDY KAINFEILEV QY
//
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