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Database: UniProt
Entry: A0A373LG12_9FIRM
LinkDB: A0A373LG12_9FIRM
Original site: A0A373LG12_9FIRM 
ID   A0A373LG12_9FIRM        Unreviewed;       787 AA.
AC   A0A373LG12;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=alpha-galactosidase {ECO:0000256|ARBA:ARBA00012755};
DE            EC=3.2.1.22 {ECO:0000256|ARBA:ARBA00012755};
GN   ORFNames=DW006_10590 {ECO:0000313|EMBL:RGF48746.1};
OS   Eubacterium sp. AF36-5BH.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=2293108 {ECO:0000313|EMBL:RGF48746.1, ECO:0000313|Proteomes:UP000262191};
RN   [1] {ECO:0000313|EMBL:RGF48746.1, ECO:0000313|Proteomes:UP000262191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF36-5BH {ECO:0000313|EMBL:RGF48746.1,
RC   ECO:0000313|Proteomes:UP000262191};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-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   -!- 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:RGF48746.1}.
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DR   EMBL; QTVG01000010; RGF48746.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A373LG12; -.
DR   OrthoDB; 9758822at2; -.
DR   Proteomes; UP000262191; Unassembled WGS sequence.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
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   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000262191}.
FT   DOMAIN          26..280
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   DOMAIN          653..783
FT                   /note="Glycosyl hydrolase family 36 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16874"
FT   ACT_SITE        474
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   ACT_SITE        544
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         362..363
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         439
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         472..476
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         522
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         544
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ   SEQUENCE   787 AA;  90625 MW;  1C7B324F090B8ED1 CRC64;
     MIKKLENGFI LNTKNTTYAF RVLKTGHLEH LYYGKKIAIE NMEPLIEQHN FMPGNTVAYN
     QETMEYSLEN MRLEMSSYGK GDVREPFVEV VKSDGSFTND FTYADSEISW GKQPFETLPG
     SYDEDGNVDH LTVTLKDNDL VMELHYYVYE NCDVITRSTV LINKGKEKVN IKRLMSMQLD
     MFGMNYVMTT FNGSWANEMN RHDTKVAAGR FANYSYAGTS SNRANPFVMI SREETTEDFG
     ECIGTNLIYS GNHYEAMDVC SFNKTRFVSG INPQSMSYGL LPGEKFEAPE SVLTYSKKGY
     NGMSQNMHKF VREHIVRGKW KYKERPVLLN SWEANYFDIT EEKLINLAKA GKDIGIELFV
     MDDGWFGKRN DDTSSLGDWY VNKDKLPNGL AHLVDEINKI GLDFGIWIEP EMINKNSELY
     KKHPNWVLEN PNAHHSEGRN QCMLDLTNNE VVDYMVKEIS NILSSANISY VKWDMNRIFS
     DYYSAGLPYE SQGEVSHRYV LGFYKMAKAL TEKFPEILFE GCCGGGNRFD LGMLCYFPQI
     WASDDTDAVC RVNIQNGYSY GYPMSTVGAH VSACPNHQTL RTTPIDTRYN VACFGVLGYE
     CDLTKMSKED LFLIKKQIEE YKKWRKVLQF GEFYRGKSPY ENSQDSDSNN VYQWTCVSAD
     KKKAVGMLFR KIIKPNDQFL NFRPKALAEN KEYHFYNRPV YHNKKDMGHF VYENNEIKSN
     ENLSKDEVSF VAENFVKGET EDYIAYGSLL NEAGVNLKEG FAGIGVNGDT RIMKDFDSRL
     YYMEEVE
//
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