ID A0A2M9H9I4_9BIFI Unreviewed; 773 AA.
AC A0A2M9H9I4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=CS006_05410 {ECO:0000313|EMBL:PJM73473.1};
OS Bifidobacterium primatium.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2045438 {ECO:0000313|EMBL:PJM73473.1, ECO:0000313|Proteomes:UP000229095};
RN [1] {ECO:0000313|EMBL:PJM73473.1, ECO:0000313|Proteomes:UP000229095}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRE1 {ECO:0000313|Proteomes:UP000229095};
RA Mattarelli P., Modesto M., Puglisi E., Morelli L., Spezio C., Bonetti A.,
RA Sandri C.;
RT "Draft genome sequences of strains TRE 1, TRE 9, TRE H and TRI 7, isolated
RT from tamarins, belonging to four potential novel Bifidobacterium species.";
RL Submitted (OCT-2017) 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:PJM73473.1}.
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DR EMBL; PEBI01000002; PJM73473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9H9I4; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000229095; 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:UP000229095}.
FT DOMAIN 20..285
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 658..763
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 481
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 551
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 366..367
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 446
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 479..483
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 529
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 551
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 773 AA; 85779 MW; C1229D8FCBB80BED CRC64;
MRFHMTNGLI SHVIQVLPNG DLNTLYFGSA IHDRMDFSDL QELDVRDTMQ VDADHPGISL
EQIRREYPQA GSSDLRPCAL SVRNAAGSQA VKLAYETYRI VHGKVSLDGL PSTFANIATD
NVEESGQADC ETLEIDLVDA SFGLKVTLSE TMFRGLPVVA RSVRIRNLSH LPQTVEAAYS
ASLDLPDADW DMITLTGAWA RETHVERAPL RTGLQGVSSI RGHSSQHASP YIALARPNAD
EMQGESVAAT LVYSGNFDAS VFVDSYARTR LRIGINPETF SWRLAPGGTF RTPEAIIACS
RTGLNGLSQT LHALYRRNLI RSPWNTRRSP IVVNTWEAVH MDMDEASLTA MARSAKDLGM
EMLVVDDGWF GHRDRADSSL GDWFADRRKF PNGLKSLADA VHDMGMGFGL WFEPEMISED
SDLFHRHPDW VLGDPRLPLR SLGVQRCQYV LDMTRPEVVD YLLQAMGNAI GRIGVDYVKW
DMNRSLSEAY SRALPPDRQG EVFHRHALGY YQLLHGLAAR FPNLFIESCA SGGARVDAGT
LATAPQAWIS DDTDALERVK IQYGTSMLYP VGACSNHVSA IPNEETGRRL SLKMCGDVAL
FGAFGYELDP TVLDEDERKR IRRQIAWAKW LGPLMRTGTF WRLRSPFDRR PGFDAADAAW
MMVADDGRMA VVGWYRALTG VNAPVPWLRL AGLQDDVRYA VTEIDTTVAD ADDTAMAGRG
FTPWRPRYGD ELMRAGLPLT DRTTATWGRS PLPGDGFSRI FILTAIPTAN TSL
//
