ID A0A0Q4GWF7_9SPHI Unreviewed; 728 AA.
AC A0A0Q4GWF7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=ASE74_18145 {ECO:0000313|EMBL:KQM77179.1};
OS Pedobacter sp. Leaf216.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1735684 {ECO:0000313|EMBL:KQM77179.1, ECO:0000313|Proteomes:UP000051744};
RN [1] {ECO:0000313|Proteomes:UP000051744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA Garrido-Oter R., Mueller D.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf216 {ECO:0000313|Proteomes:UP000051744};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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}.
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:KQM77179.1}.
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DR EMBL; LMKM01000007; KQM77179.1; -; Genomic_DNA.
DR RefSeq; WP_055906120.1; NZ_LMKM01000007.1.
DR AlphaFoldDB; A0A0Q4GWF7; -.
DR STRING; 1735684.ASE74_18145; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000051744; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..728
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006219528"
FT DOMAIN 44..279
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 637..714
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 542
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
SQ SEQUENCE 728 AA; 83724 MW; 251FF50721B2A79C CRC64;
MTKTHFTLYF LLIASTVTCF AQKTIEIATK NNVLILETDK DNALLSTYIG KRLQSTEEYP
NIQALDKYKP GSDDLLNKRE AYIASGSLNL MEPALSVTHS DGNKSTVLSF SEVKTEQIDQ
NRKLTSIVLK DFKYNFKVTL KYLAYFNEDV IEQWAEIEHH EKKSIVLNKY ASANLTLSGR
KFFLKNQYSG ATREMRSEEQ QLLHGIKTID SKLGTRTNLL HSSSFMVSID QPANEDLGEV
IAGSLAWTGN FKLDFETFDE YYLRITAGIN NFSSNYTLKA GENFVTPRFI YTYSSEGKGL
ASRNLQNWAR NYQILDGKGE RSTILNNWET TYFDFNDEKL NELTKDTKKL GVDVFLLDDG
WFGNKYPRNG STSGLGDWQY NRQKLKNGIS TLGKEATASG VKFGIWIEPE MVNPKSELYE
NHPDWILRQP ERKEYYMRNQ LVLDLTNPKV QDFIFNTVND IFKEVPELAF IKWDCNSLIY
NANSPTLKNQ DHFYIEYIRG LNNVLERIRK KYPKTPMMLC AGGGSRVDYA ALKYFTEFWP
SDNTNPYDRI FIQWEYSYYF PSVAVDNHIT DMGKQPIKFK TDVAMMGKLG YDVRVNELSS
NDLLFSKNAV KTYNNFKEIV WHGQQYRLQD PYENKIASIA YINDAKDQAI VFNYYVATLF
TNGVILPIKL KGLDPAKKYK IEEINLYPGT KSPIDATKVY SGDFLMKVGF NPEANSYRTS
VVLKVQAI
//
