ID A0A1K2FNA0_9ACTN Unreviewed; 547 AA.
AC A0A1K2FNA0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Alpha-galactosidase {ECO:0000256|RuleBase:RU361168};
DE EC=3.2.1.22 {ECO:0000256|RuleBase:RU361168};
DE AltName: Full=Melibiase {ECO:0000256|RuleBase:RU361168};
GN Name=agaA {ECO:0000313|EMBL:SFY49283.1};
GN ORFNames=STEPF1_02516 {ECO:0000313|EMBL:SFY49283.1};
OS Streptomyces sp. F-1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=463642 {ECO:0000313|EMBL:SFY49283.1, ECO:0000313|Proteomes:UP000095403};
RN [1] {ECO:0000313|EMBL:SFY49283.1, ECO:0000313|Proteomes:UP000095403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Streptomyces sp. F1 {ECO:0000313|EMBL:SFY49283.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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|RuleBase:RU361168};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
CC {ECO:0000256|ARBA:ARBA00009743, ECO:0000256|RuleBase:RU361168}.
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DR EMBL; FKJI03000005; SFY49283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1K2FNA0; -.
DR Proteomes; UP000095403; Unassembled WGS sequence.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14792; GH27; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 3.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR041233; Melibiase_C.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE; 1.
DR PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17801; Melibiase_C; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|RuleBase:RU361168};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361168};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361168};
KW Reference proteome {ECO:0000313|Proteomes:UP000095403};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 415..547
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 547 AA; 56950 MW; DD4CBBE5761D0DAB CRC64;
MPAHIPPARR RLRHLARRSR MLALTAAGAL LAFALPLVTV GTAQPAAALG NGLALTPQMG
FNDWNAYGCN VSESLIKSTA QAMHTNGMQA AGYTYVNIDD CWMTHSRDSS GRLVPDPAKF
PDGIKGTADY VHSLGLKLGI YEDAGTATCA GYPGSLGHET TDAQSFASWG VDYLKYDNCN
NNGVAAQTRY TAMRDALAAT GRPILYSLCN WGQDNVWTWG ANVGNSWRTT GDITASYSSM
LSIFHSNVGL ASYAGPGHWN DPDMLEVGNS GLSDTEARSE FSLWAEMAAP LIAGTNLTSA
SSATLATYTN SRVIAVDQDS LGRQGTLVSS SNGLDVLAKP LANGDVSVVL FNETGSTATI
STTANAVGKT GAAGYTLTDL WSGATSTTSG TISASVPAHG VVMYRVAGGS STGGGDATGE
IHAVGAGKCL DVPDSATTAG TQVEIWTCGG GANQLWTHTS SQQLTVYSGS SQMCLDAYDN
QTAPGTKVEI WQCNGQTNQQ WRINSDGTIT GVQSGLCLDV TGGSTANGAL AELWTCNGQT
NQQWNLG
//
