ID A0A0C5VK42_9GAMM Unreviewed; 556 AA.
AC A0A0C5VK42;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=YC6258_03014 {ECO:0000313|EMBL:AJQ95052.1};
OS Gynuella sunshinyii YC6258.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Gynuella.
OX NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ95052.1, ECO:0000313|Proteomes:UP000032266};
RN [1] {ECO:0000313|EMBL:AJQ95052.1, ECO:0000313|Proteomes:UP000032266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC6258 {ECO:0000313|EMBL:AJQ95052.1,
RC ECO:0000313|Proteomes:UP000032266};
RA Khan H., Chung E.J., Chung Y.R.;
RT "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT YC6258T gen. nov., sp. nov.";
RL Submitted (JAN-2014) 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; CP007142; AJQ95052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C5VK42; -.
DR STRING; 1445510.YC6258_03014; -.
DR KEGG; gsn:YC6258_03014; -.
DR PATRIC; fig|1445510.3.peg.2982; -.
DR HOGENOM; CLU_013093_3_3_6; -.
DR Proteomes; UP000032266; Chromosome.
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; -; 2.
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:UP000032266};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 433..556
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 556 AA; 60190 MW; D697C408759072BF CRC64;
MLNQRKFNRS IVRKKHRESC DAVGRFSRIV MTFFAILFVS SQWPAYALDN GVSRTPPMGW
NTWNTFGCNI NESLIRQMAD SIVSSGMADA GYKYVVVDDC WFNPNRDSAG NLQSDPSRFP
SGMKALGDYL HSKGLKFGIY QVPVDKTCAQ YFSSYPGATG SQGHEYQDAQ QFAAWGVDYL
KYDWCSPNGS IDDQVTAFAK MRDALASTGR PIVYSINPNS IHEKTGPMRN WGDVANIWRT
TEDITSSWDT GQTNGYPMGV KNIVDVTARL AAYAAPGSFN DPDMMEVGIG SMSDTEMRSH
FALWAIMASP LIAGNDIRNM SWATRTILTN SNLIAINQDT LGLQGVEIQN DGTRRVMVKK
LANGDVAVAL FNQGNSATTI TTTAAAIGKS GSDFNLLDAW SGTTSSTSGV ISANVPAHGT
VVYRVSGGSA LAGTSLVSAS ASRCLDDPNS ATANGTNPII WSCSGASNQR WEISGKTIQV
LGKCLDVALD ASAGSNVQLW DCNGGSNQNW IFNTDGTVRN ESNGLCLDVY NNETANGTEV
ILWYCGNVAN RRWAKL
//
