ID A0A1H8XJV9_9SPHI Unreviewed; 722 AA.
AC A0A1H8XJV9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN05428947_11477 {ECO:0000313|EMBL:SEP40003.1};
OS Mucilaginibacter sp. OK283.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1881049 {ECO:0000313|EMBL:SEP40003.1, ECO:0000313|Proteomes:UP000199509};
RN [1] {ECO:0000313|EMBL:SEP40003.1, ECO:0000313|Proteomes:UP000199509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK283 {ECO:0000313|EMBL:SEP40003.1,
RC ECO:0000313|Proteomes:UP000199509};
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; FODR01000014; SEP40003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8XJV9; -.
DR STRING; 1881049.SAMN05428947_11477; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000199509; 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 57..269
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 629..706
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 464
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 533
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 348..349
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 428
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 462..466
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 511
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 533
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 722 AA; 82618 MW; 5FD686D1DF488495 CRC64;
MSKLVLFIYL AFFCGGTVLK AQSNKQIIIA TKNVNLVFTV GANNRVYQAY LGKRFLNQAD
NSLIPNNKHE AYIAGGMEDL LQPAIRLIHS DGNPSLELRY VNHTTKNSDQ NISETNILLQ
DPKYPVQVIL HYQAFSEEDI IKSWAEIKND EKGEINVENY ASSMLHFEAK DYWLTQFHGD
WASEMKMQES KLTSGVKEID SKLGTRADMY QTPVFFLALN KPADETTGEL IAGTLAWTGN
FQFHFEIDER NALRVISGIN PYASAYKLKK GETFTTPAFI FTYSTTGKGQ ASRNLHQWAR
NYGVLDGNKP RLTLLNNWEA THVNFNEKEL VGLFDDATKL GVDLFLLDDG WFGNKYPRDN
DKAGLGDWQE SKAKLPNGIG YLVKQAEAKG LKFGIWLEPE MVNPKSELYE QHLDWILKLP
NRDENYQRNQ LVLDLTNPKV ADYVYHTVVD MLTKNPGLAY IKWDCNRSMS NTWSPYLKDR
QSALFVDYTL SLYKILDRIR QKYPHLPIML CSGGGGRTDY GALKYFTEFW PSDDTDPLER
VYIQWGYSNF FPALTISSHV TSWGKQSIKF HTDVAMMGKL GYDIKVSKMT DDELQFSKQA
VKNYNRLSNT IWFGDLYRII SPYDENRMVA MYVNAEKSKA VLFNYNLNTR YKEVFNRVRL
QGLDSQKKYK VEETNLMPGA KSNLAENGRV FSGDYLMTMG LNLTPGKLIP LTSMVIEINA
EN
//
