ID A0A1H9RZC9_9ACTN Unreviewed; 729 AA.
AC A0A1H9RZC9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05443377_11059 {ECO:0000313|EMBL:SER78018.1};
OS Propionibacterium cyclohexanicum.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=64702 {ECO:0000313|EMBL:SER78018.1, ECO:0000313|Proteomes:UP000198815};
RN [1] {ECO:0000313|EMBL:SER78018.1, ECO:0000313|Proteomes:UP000198815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16859 {ECO:0000313|EMBL:SER78018.1,
RC ECO:0000313|Proteomes:UP000198815};
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; FOGZ01000010; SER78018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9RZC9; -.
DR STRING; 64702.SAMN05443377_11059; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000198815; 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 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; IPR031704; Glyco_hydro_36_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43053:SF3; ALPHA-GALACTOSIDASE C-RELATED; 1.
DR PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 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:UP000198815}.
FT DOMAIN 28..273
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT ACT_SITE 463
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 530
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 351..352
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 461..465
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 508
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 530
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 729 AA; 80151 MW; 21F54D625AB925AF CRC64;
MILGPQTQLA HLHASKTSIV IDVSSGRDPA IVYWGADLGN VSSAVLEAMV RAGLDPTVGS
SVDGGVRLGA LALSSSGWSG RPGLAGHRDD GTAWAPALGV DEVLLDAAEI AVDAAAVSAG
AGRLRCSMVD PDCGLRAELI VELLATGLIR VRAEVTNEAA EDWTVDELAV VLPVPLQADE
LLDFSGRWSH ERVPQRRHLD LGNWLRESRH GRTGFDSPTM SFCGEPGFDQ ASGQVWGLHV
GFSGNQRCWV ERRPEGRQVM AGGELLLPGE VRLAQGQGYR SPWVYAVHAD GLDDAAHRVH
DWLRSLPGHP ATPRPVTLNV WEAVYFDHDE QTLLSLAERA AAIGVERFVL DDGWFLGRRN
DTAGLGDWVV DPQVWPAGLH PLVDHVRELG MQFGLWFEPE MINIDSELAR AHPDWIMATG
ARLPVEWRHQ QVLGLAIPEA FDHVHAAIGA ILDEYDISYI KWDQNRDLID AGDRQRGGRP
VVHEQTLACY RLMDALRAEH PGLEIESCSS GGGRIDLEMA RHAQRFWISD CIDPHERAQI
MRWTEQIIPP EMMGTHLASP RNSITGRVSE LSFRAGMAIW GHFGVEWNLL ETTDDEMSRL
SEWIAFYKDE RALLCTGDLV RRDLGGALLL HGVVARDRLR ALYGLIRLES TALAQSGQVL
IPGLDDHASY RLRPRLVGNG PERLGEPAWF GVDHEGIVMT GQALRLHGVR APQLLPDQIL
ILEATRTAG
//
