ID A0A1H9R125_9SPHI Unreviewed; 736 AA.
AC A0A1H9R125;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN04488023_11355 {ECO:0000313|EMBL:SER65749.1};
OS Pedobacter rhizosphaerae.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=390241 {ECO:0000313|EMBL:SER65749.1, ECO:0000313|Proteomes:UP000199572};
RN [1] {ECO:0000313|EMBL:SER65749.1, ECO:0000313|Proteomes:UP000199572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18610 {ECO:0000313|EMBL:SER65749.1,
RC ECO:0000313|Proteomes:UP000199572};
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; FOGG01000013; SER65749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9R125; -.
DR STRING; 390241.SAMN04488023_11355; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000199572; 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:UP000199572};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..736
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011657758"
FT DOMAIN 51..285
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 644..730
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 480
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 197
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 364..365
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 478..482
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 736 AA; 84047 MW; 8214AF959DBAA26E CRC64;
MYRSVRLRKV SRATVLLVSL LFTGKLSKAQ TIIPIETENQ ALVLKAVNGG DVTIQYFGQK
LVSTKEYGLI GGTYKQTEDY TGQLNSVYTP SGSRNLLEPA ISVVHSDGNN SLNLSYVSHE
TRKINDNTSL TKILLKDPAY NFQVELYYQS YFKENVFEQW TEIKHQEKGN VILQKFASAN
LHLKAKDYYL KQYHGDWALE MQPEESRITH GIKTLDSKLG TRANLFQPSV FMVSLDAPAT
ENNGSVLYGA MEWSGNFRID LEVDYQDNLR IIAGMNNYAS PYKLKPNEAF VTPKFLYTFS
NQGKGAASRQ LQNWARNYQI LDGKGDRLTL LNNWEATYFD FNEQVLAALL KDTKKLGVDL
FLLDDGWFGN KYPRNSDRVG LGDWQENKSK LPNGISSLVK EAEGNAVKFG IWIEPEMVSP
KSELYEKHPS WVIKQPKRAE HYFRNQLVLD LSNPEVQDFV FGIVDGLFTK NPSLSYIKWD
CNAVIYNAYS AHLKENQAAF YIDYVKGLYR VLERIRTKYP KVPMMLCSGG GGRVDYAALK
YFTEFWPSDN TDPMERIFMQ WEYSYFYPAI SSANHVTDWG KQPIKFRTDV AMMGKLGFDI
VVSKLPEKDL LFCQEAIKNY NVLKTDIWQG DQYRLANPRE GSVAAMLYLN ADKASGVVFN
YLVNNRYEEK SKLPIKMQGL NPNKNYKLTE INLYPGTKST LDATQVYSGD FLTKIGYNPN
VNASRTSVVL KLEEVK
//
