ID A0A1I5EX45_9CLOT Unreviewed; 775 AA.
AC A0A1I5EX45;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN04488695_12225 {ECO:0000313|EMBL:SFO16064.1};
OS Proteiniclasticum ruminis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Proteiniclasticum.
OX NCBI_TaxID=398199 {ECO:0000313|EMBL:SFO16064.1, ECO:0000313|Proteomes:UP000181899};
RN [1] {ECO:0000313|EMBL:SFO16064.1, ECO:0000313|Proteomes:UP000181899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML2 {ECO:0000313|EMBL:SFO16064.1,
RC ECO:0000313|Proteomes:UP000181899};
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.
CC {ECO:0000256|PIRNR:PIRNR005536}.
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DR EMBL; FOVK01000022; SFO16064.1; -; Genomic_DNA.
DR RefSeq; WP_074913290.1; NZ_FOVK01000022.1.
DR AlphaFoldDB; A0A1I5EX45; -.
DR STRING; 398199.SAMN05421804_101592; -.
DR eggNOG; COG3345; Bacteria.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000181899; 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:UP000181899}.
FT DOMAIN 26..279
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 642..767
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 472
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 540
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 360..361
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 437
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 470..474
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 540
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 775 AA; 89421 MW; 7EBCA8880341794F CRC64;
MIEVRQKVFR LSTKSTSYLF RILPTGHLEN LHYGRLLAWQ DFQGLYMKQN AGVGSSVLYE
EGGYTLDLLP LEYSFNGKGD FREMPFEIKM PDGSYVCDFH YESHEILEGT LPMEEMPTAK
GEEAETLVVH LRDTLHPLRM TLVYTVFSNC DVITRRAVIE NRSDQPVEIL KFMSMQLDLL
MDHPEVLTLS GGWIREAQKE RHRLPVGSFL QESRTGGSSN RHNPGLLLME KNATEDFGKV
YGFNLLYSGN HRSVVEKTSH GLVRVHQGIS PHNFSWVLES GETFRTPEAV MTVSMDGMNG
VSHHFHDFIN RHIISKEFQY KERPVLMNNW EATFFDFNER KILSLAREAK KLGVELFVLD
DGWFGERNSD RAGLGDYGEN RKKLPSGIKG LAEKIKAMGL DFGLWFEPEM VNEDSDLYRN
HPEYALQVPG RTPSKGRHQL VLDINRREVQ DYIIKEVSHL LESCDISYVK WDMNRHMSDV
YSDAVNHQGM AFHGHILGLY RVLKILTERF PKVLFESCSS GGNRFDLGML SYMPQVWASD
NTDPISRLSI QEGLSYFYPL STIGAHVSES PHQQTLRKTP LETRFHVASF GVLGYELELT
HLNLKEKEEV KKQIAWYKKY RSLMQFGRFY RFDSVRENRV NFQVVSEDRK KTVQGFFQKM
QEPSPPFDVM PFKGLHHENT YVVRTREASM DIEVFGSLLK HVMPIKLSPG GLILRNARKL
YRLPHNVEEY TAKGDLLSEG LRIHQQFMGT GYQKDTRMLG DFGSQLMVGE MKEEN
//
