ID A0A2V1ILC3_9BACT Unreviewed; 736 AA.
AC A0A2V1ILC3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=C5O23_03820 {ECO:0000313|EMBL:PWB03283.1};
OS Duncaniella muris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae;
OC Duncaniella.
OX NCBI_TaxID=2094150 {ECO:0000313|EMBL:PWB03283.1, ECO:0000313|Proteomes:UP000244905};
RN [1] {ECO:0000313|Proteomes:UP000244905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103720 {ECO:0000313|Proteomes:UP000244905};
RA Clavel T., Strowig T.;
RL Submitted (FEB-2018) 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:PWB03283.1}.
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DR EMBL; PUEC01000006; PWB03283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1ILC3; -.
DR Proteomes; UP000244905; 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; 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.
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:UP000244905};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..736
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016177288"
FT DOMAIN 43..270
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 639..731
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 467
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 537
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 349..350
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 465..469
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 515
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 537
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 736 AA; 82904 MW; FAB209B8C855C92A CRC64;
MKQFLLLPGA ALLLMTAALP ATAETVNIST PNTSLVLDAE KGGKLRILHY GNRLSDADIA
NLSEAGAIRR DAYPVYGIYP QAEAAMSVTH ADGNRTTDTE VTGITSRKDA DGADVTTIAM
RDKVYPFDLN VNYRTYPGED VIETWVDVKN NEKGTVTLNR FMSGYLPVRY GNVWLSQLYG
SWANEGKVSE TPLNHGVRMI KNKDGVRNSH TSHAEIMLSL DGKPQENTGR TVGAALEYSG
NYKLFIDTDD SDYHHFFAGI NEENSEYHLK TGESFVTPPL ALTYSEEGLS GVSRNFHRWG
RNHRLHAGNT ERKVLLNSWE GVYFNITEPV MDGMMKDIAD MGGELFVMDD GWFGKKYPRD
NDSTTLGDWV VDTNKLPNGI QALIDSASTH GIKFGIWIEP EMTNTVSELY EKHPEYIIKA
ANRPATQGRG GTQLVLDLAN PKVQDIVFTV VDTLMRKYPA IDYIKWDANA PIMDHGSQYL
TADNQSHLYI DYHKGFETVL NRIRKAHPDV TIQACASGGG RANWGILPWF DEFWTSDNND
ALQRIYMQWG TSYFFPAIAM GSHISASPNH QTFRRIPVKF RADVAMSGRL GLEMQPRDMN
DEDKAVCRQA ITDYKKIRPI VQFGDIYRLI SPYDGKGVAS LMYVTPEKDD AVFYWWKTET
FMNQQLPRVV MAGLDPDKIY MITELNRIDK EPLSFEGKTF SGRYLMSNGL EIPLTHKVDY
HKNTDYASRV LRVTAK
//
