ID A0A3N2BBZ0_9MICO Unreviewed; 721 AA.
AC A0A3N2BBZ0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=EDD31_1130 {ECO:0000313|EMBL:ROR72771.1};
OS Bogoriella caseilytica.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Bogoriella.
OX NCBI_TaxID=56055 {ECO:0000313|EMBL:ROR72771.1, ECO:0000313|Proteomes:UP000280668};
RN [1] {ECO:0000313|EMBL:ROR72771.1, ECO:0000313|Proteomes:UP000280668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11294 {ECO:0000313|EMBL:ROR72771.1,
RC ECO:0000313|Proteomes:UP000280668};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-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:ROR72771.1}.
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DR EMBL; RKHK01000001; ROR72771.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2BBZ0; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000280668; 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:UP000280668}.
FT DOMAIN 30..266
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 627..706
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 457
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 523
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 344..345
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 422
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 455..459
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 501
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 523
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 721 AA; 79773 MW; DE2BC0C62FEF95F1 CRC64;
MTTPSHALPD HVHLQAAGVS LLLDCAEGHL PRVLHWGHSL GAITEHDIEH LRLAARPPAG
AAQVDAAVHL SVLAEQSAGW PGTPGLTGHR EGADFSTAFR VTAIEHAAGD GFSMAERAVI
TATDAPSGLD LTLEIELSSS GLARMRAAVT NREDRAFSLH SLDLNLPVPT EAQEILDFTG
RWARERSPQR HAFTLGTHLR ENRRARALDV SSLMAAGPTG FGWRSGEIRA LHVGWSGNTR
LYAERHHHAV ALLAGGELLH AGEVQLGRDE TYTGPWLYFS HGDGLDEMAG RFHQYLRQRP
EHPTSPRPVQ INVWEAVYFD HDLEKLKQLA DVAASLGVER YVLDDGWFGS RRDDSSGLGD
WVVSPEVWPH GLWPLVDHVR GLGMEFGLWF EPEMVNPDSE LARAHPEWIL AARPERWPLE
ARQQQVLDLT IPEAYAHVRD QMLAIVEEYP ISYIKWDYNR DLTEPGNQAS GRAVVHEQTR
AVYHLMDELL AAKPGLEIES CSSGGGRIDL GVMERCVRVW ASDCIDPLER QQIEAGTSLL
LPPELVGSHV ASTVNHTTGR HHSIDFRAST AFFSHMGIEW DLTSATEEEL SRLGDWIALY
RQNRELLHSG SVVHADHPDE SLTLQGVVGA DQERALYALT ALRTSPFTTP GMVRLPGLDP
ERRYRVRPLL PGGADAAPTE ARTAWWLEGT TLPGRVLATT GIQLPQLNPE QRLLLEVRTE
E
//
