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Database: UniProt
Entry: A0A0R2KCR6_9LACO
LinkDB: A0A0R2KCR6_9LACO
Original site: A0A0R2KCR6_9LACO 
ID   A0A0R2KCR6_9LACO        Unreviewed;       737 AA.
AC   A0A0R2KCR6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=IV43_GL001770 {ECO:0000313|EMBL:KRN87234.1}, LAC1533_0550
GN   {ECO:0000313|EMBL:SFV39970.1};
OS   Ligilactobacillus acidipiscis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=89059 {ECO:0000313|EMBL:KRN87234.1, ECO:0000313|Proteomes:UP000051491};
RN   [1] {ECO:0000313|EMBL:KRN87234.1, ECO:0000313|Proteomes:UP000051491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15353 {ECO:0000313|EMBL:KRN87234.1,
RC   ECO:0000313|Proteomes:UP000051491};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
RN   [2] {ECO:0000313|Proteomes:UP000190935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACA-DC 1533 {ECO:0000313|Proteomes:UP000190935};
RA   Papadimitriou K.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SFV39970.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACA-DC 1533 {ECO:0000313|EMBL:SFV39970.1};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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 36 family.
CC       {ECO:0000256|ARBA:ARBA00006202}.
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DR   EMBL; JQBK01000006; KRN87234.1; -; Genomic_DNA.
DR   EMBL; LT630287; SFV39970.1; -; Genomic_DNA.
DR   RefSeq; WP_010497197.1; NZ_LT630287.1.
DR   AlphaFoldDB; A0A0R2KCR6; -.
DR   STRING; 89059.LAC1533_0550; -.
DR   KEGG; laca:LAC1533_0550; -.
DR   PATRIC; fig|89059.3.peg.1887; -.
DR   OrthoDB; 9758822at2; -.
DR   Proteomes; UP000051491; Unassembled WGS sequence.
DR   Proteomes; UP000190935; Chromosome i.
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}.
FT   DOMAIN          39..293
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   DOMAIN          657..733
FT                   /note="Glycosyl hydrolase family 36 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16874"
FT   ACT_SITE        486
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   ACT_SITE        556
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
SQ   SEQUENCE   737 AA;  84075 MW;  EE0F755D86CFBEAF CRC64;
     MTKPSAKSEL IEVSSNPLTF HLHNSQVSYV LGVEDENILA HHYYGKAVDH YSNLRRYPRL
     MRHFAPSPED IETRDFSLST LPQEFPGAGG ADYREPGIVV QFPNGSRTVN FTYDSYTISD
     GKPQLAGLPA TFAQEDEAQT LTVKLVESDA QLELYLSYTI FRDLPVITRS ARVKNLGQQP
     VQVQRLVSFS LDSPDNELNL LQLNGRYAQE RNVTIEPLNT GIKILDSKRG ASGHTQNPFC
     ALIDPHATEF SGEVFGFCLV YSGSHKSIIQ MDGYNQVRIQ MGINDQNFEW WLEPQKSFQS
     PEAVLVHSEQ GLNSMSQSFH ELFLNHLMKS KYSHQTRPIL LNNWEATYFN FDEKKLQDII
     ASSHDLGIEM FVLDDGWFGE RDAPNSSLGD WVVDRKKLPN GLKPLSDYCH NLDMKFGLWF
     EPEMISVKSK LYQSHPDWVL EVPGQRRSID RSQFVLNLGR AEVRDYLLER MSYIIEHADL
     DYIKWDMNRN MTEVYDAKLS ASEQGEVSHR YILGLYDLLE RLTDNYPDIL FESCSGGGGR
     YDAGMLYYMP QTWTSDNTDA IARLKIQYGT SLVYPVVSMG AHVSAVPNEQ TGRMTPLRTR
     GLVASSGNLG YELNPLNLLE NERQEVKLQV KWYKAHRRLI QFGKLYRLQN PFETTRTAWM
     FVSDDKKEAV AMYFNIFSEA SSPLHMLNFV GLNPSQKYSV NGEYTAYGSE LMQIGIYPLT
     QNDGDFDSAV FELKAVE
//
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