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Database: UniProt
Entry: A0A1I4IJ10_9BACI
LinkDB: A0A1I4IJ10_9BACI
Original site: A0A1I4IJ10_9BACI 
ID   A0A1I4IJ10_9BACI        Unreviewed;       742 AA.
AC   A0A1I4IJ10;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=SAMN04487943_102119 {ECO:0000313|EMBL:SFL53801.1};
OS   Gracilibacillus orientalis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX   NCBI_TaxID=334253 {ECO:0000313|EMBL:SFL53801.1, ECO:0000313|Proteomes:UP000198565};
RN   [1] {ECO:0000313|EMBL:SFL53801.1, ECO:0000313|Proteomes:UP000198565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.4250 {ECO:0000313|EMBL:SFL53801.1,
RC   ECO:0000313|Proteomes:UP000198565};
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|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; FOTR01000002; SFL53801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4IJ10; -.
DR   STRING; 334253.SAMN04487943_102119; -.
DR   OrthoDB; 9758822at2; -.
DR   Proteomes; UP000198565; 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}.
FT   DOMAIN          31..286
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   DOMAIN          650..738
FT                   /note="Glycosyl hydrolase family 36 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16874"
FT   ACT_SITE        479
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   ACT_SITE        549
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         367..368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         444
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         477..481
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         527
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         549
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ   SEQUENCE   742 AA;  86444 MW;  4289F6ED85E84AE7 CRC64;
     MPIQVNEEQL EFHLYNDNVS YIFRVLEKSH QLEHLYYGKR IHHRKSFAHL IEREIRPSTN
     MFEGDHTSSM EHIKQEYPSY GSTDFRYPAH TILRQDGSHI TDFTYDSFRV INGKKPLTDL
     PATYVENEDE ADTLEIELVD DILQCRLILS YTIYQNRNVI TRHAKFINEG LESYYLDQAM
     SMNIDLPDDQ FDMLHLQGAW AREGHVETKR LSKGIQSIYS NRGGSSHVFN PFFALKRWNT
     DENQGEVYGF SLVYSGNFLA QIEVDTYNVS RVNMGINPYR FKWKLASGGS FQTPECVMVY
     SDQGLNGMSQ TFHKLYRERL VRGYWRDKVR PILINNWEAT YFDFNEEKVL NIAKTAQELG
     IELFVLDDGW FGKRDDDTSS LGDWFEYEEK LPNGIDGLSE KVEALDMRFG LWFEPEMVCK
     DTKLFEKHPD WIISTPERRA SHGRNQFVLD FTRTEVVDYI FDLMDKIISK SNISYIKWDM
     NRHITEAFSQ NLPADQQGEV FHRYILGVYD LYERLIKKYP EILFESCAGG GARFDPGMLY
     YAPQTWTSDD TDAVERLKIQ YGTSMVYPLS AIGSHVSAIP NHQVGRLASL DTRAAVAYFG
     TFGYELDITQ LTEEEKQKVK EQVAFFKEKR SLIRDGEFYR LSSPFEYNET TWMVVNEEKS
     EAIVGYYKVL AKPNEAYNRI KLTGLDPEKL YEINGENSYY GSELMNVGIV LAGNFIDRAD
     EYWGQEHPGD YQSRLFILKA LS
//
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