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Database: UniProt
Entry: A0A0R1QG32_9LACO
LinkDB: A0A0R1QG32_9LACO
Original site: A0A0R1QG32_9LACO 
ID   A0A0R1QG32_9LACO        Unreviewed;       755 AA.
AC   A0A0R1QG32;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=FD01_GL001667 {ECO:0000313|EMBL:KRL43521.1};
OS   Lacticaseibacillus manihotivorans DSM 13343 = JCM 12514.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1423769 {ECO:0000313|EMBL:KRL43521.1, ECO:0000313|Proteomes:UP000051790};
RN   [1] {ECO:0000313|EMBL:KRL43521.1, ECO:0000313|Proteomes:UP000051790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13343 {ECO:0000313|EMBL:KRL43521.1,
RC   ECO:0000313|Proteomes:UP000051790};
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).
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:KRL43521.1}.
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DR   EMBL; AZEU01000191; KRL43521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R1QG32; -.
DR   PATRIC; fig|1423769.4.peg.1781; -.
DR   Proteomes; UP000051790; 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:UP000051790}.
FT   DOMAIN          55..314
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   DOMAIN          675..751
FT                   /note="Glycosyl hydrolase family 36 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16874"
FT   ACT_SITE        507
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   ACT_SITE        577
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
SQ   SEQUENCE   755 AA;  84871 MW;  54460DB1E02DB398 CRC64;
     MFFTAHNPYT KQCRKRFHET GGFFMADLIA FDAKTQVFHL HNQQISYIFA IEDGGVLGHL
     YFGQAVAGYH GERHYPRKDR GFAGNLPVAD PERGFSLDTL PQEISSRGEA DFRIPAFVIC
     QADGAQASRF IYASHRIVPG KPKLPGLPAA YVESPDEAAT LIVTVVDQPS RLQADLYYTI
     YRDRAVIARS VCFRNPADQP AVTLEQAASV QLDFPAGDYR VLSLPGAHAN ERHLQKEVVG
     YGIKQFASTR GTTSHQMNNF IALTAPDADE FHGDVYGIDL VYSGNHALTV EKDQIDQVRV
     VAGINPAGFT WELAGGAEFQ TPEALLVYSH QGLNAMSQTY HRLIRERVVR GRYRDQERPI
     LVNNWEATYF NFNEAKLRPI VDAAKKLGIE MFVLDDGWFG HRDDDTTSLG DWVVDSHKFP
     LGLKHFADYV HNQGLKFGLW VEPEMISKDS DLYRAHPDYL LAVPGRAPSP SRFQYVLDLS
     REDVRANIAG QLSDLLDQGY IDYIKWDMNR HLSDIYSHAL PAARQGEVLH RYTLGLYALL
     EEMTTKYPDV LWEGCSGGGG RIDTGFAYYM PQSWTSDNTD AISRLGIQYG TSLVYPPNTF
     TAHVSVSPNE QTGRSTSLAT RGNVAMSAVF GYELDLTKLT KTEQKQVAAQ VAVYKQIRPL
     IQFGHFLRLE SGNDYAWMFV SADQNEALLF TFQLLNDGQP AFHIVKMAGL DPVKQYEDTA
     THTVYGGDEL MHMGLYQPLQ RQDFTTHQYH FKAIN
//
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