AGAL_STRMU
ID AGAL_STRMU Reviewed; 720 AA.
AC P27756;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Alpha-galactosidase;
DE EC=3.2.1.22;
DE AltName: Full=Melibiase;
GN Name=aga; Synonyms=agaL; OrderedLocusNames=SMU_877;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ingbritt;
RX PubMed=1649890; DOI=10.1099/00221287-137-9-2271;
RA Aduse-Opoku J., Tao L., Ferretti J.J., Russell R.R.B.;
RT "Biochemical and genetic analysis of Streptococcus mutans alpha-
RT galactosidase.";
RL J. Gen. Microbiol. 137:757-764(1991).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=1660918; DOI=10.1099/00221287-137-9-2271;
RA Aduse-Opoku J., Tao L., Ferretti J.J., Russell R.R.B.;
RT "Biochemical and genetic analysis of Streptococcus mutans alpha-
RT galactosidase.";
RL J. Gen. Microbiol. 137:2271-2272(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC -!- SUBUNIT: Homotetramer.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 36 family. {ECO:0000305}.
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DR EMBL; M77351; AAA26933.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58592.1; -; Genomic_DNA.
DR PIR; A44819; A44819.
DR RefSeq; NP_721286.1; NC_004350.2.
DR RefSeq; WP_002262871.1; NC_004350.2.
DR AlphaFoldDB; P27756; -.
DR SMR; P27756; -.
DR STRING; 210007.SMU_877; -.
DR CAZy; GH36; Glycoside Hydrolase Family 36.
DR PRIDE; P27756; -.
DR EnsemblBacteria; AAN58592; AAN58592; SMU_877.
DR KEGG; smu:SMU_877; -.
DR PATRIC; fig|210007.7.peg.783; -.
DR eggNOG; COG3345; Bacteria.
DR HOGENOM; CLU_009640_2_1_9; -.
DR OMA; YHDIDYI; -.
DR PhylomeDB; P27756; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR CDD; cd14791; GH36; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 2.70.98.60; -; 1.
DR Gene3D; 3.20.20.70; -; 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 Pfam; PF16874; Glyco_hydro_36C; 1.
DR Pfam; PF16875; Glyco_hydro_36N; 1.
DR PIRSF; PIRSF005536; Agal; 1.
DR PRINTS; PR00743; GLHYDRLASE36.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE 3: Inferred from homology;
KW Glycosidase; Hydrolase; Magnesium; NAD; Reference proteome.
FT CHAIN 1..720
FT /note="Alpha-galactosidase"
FT /id="PRO_0000134876"
FT ACT_SITE 472
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT ACT_SITE 541
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT CONFLICT 138..143
FT /note="LRMTLY -> SRIVSD (in Ref. 1; AAA26933)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="T -> S (in Ref. 1; AAA26933)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="E -> V (in Ref. 1; AAA26933)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="D -> E (in Ref. 1; AAA26933)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="P -> L (in Ref. 1; AAA26933)"
FT /evidence="ECO:0000305"
FT CONFLICT 502..504
FT /note="NIV -> DMF (in Ref. 1; AAA26933)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="G -> A (in Ref. 1; AAA26933)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="I -> V (in Ref. 1; AAA26933)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="I -> A (in Ref. 1; AAA26933)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 82141 MW; ED2ABF54ACFC5247 CRC64;
MGIVIKDNLF YIHTKDSSLI IEERDGDLLL KHLGKKIEAY HFSNTVFEKD HAFSANPVAD
NRNYSYDTQR QIFGVHGFGD FRVPSLILQH DNNDLTRFKF KKAKIIKGGI KARGLPNPHS
SESAQSLALI LEDDLAKLRM TLYYTAYDDN ATISTFVKFE NLSDKPVILH RALSTMFDLP
ASHYDVITFQ GAYAREKTLR RHQIEQGLFK IGSNRGASGH AQTPSLILTE HDSNEFYGEA
LALQLIYSGN FQAFVQKNQL NEVRLGIGIN DDNFSWDLQA NQSFETPVAL ITYTDKGLTD
LTQESHNFIK RHIIPKNFAN KERPILINNW EATYFDFNRS QLLGLADEAR KLGIELFVLD
DGWFGHRFDD NSSLGDWFVN EEKLGGSLDS FIKEIHDRGL QFGLWFEPEM VSVDSKLYRA
HPDWVIQADQ REHTYSRNQL VLNLANPDVV AYIKTVLDKL LTENTIDYVK WDYNRNITNI
GNGRTYLETQ MQSHAYILGL YNIVSYLTTK HDKVLFESCS GGGGRNDLGM MCYFPQVWSS
DNTDAIARLP IQYGSSYLYP TISMGAHVSA VPNHQMNRHT PLTTRGHVAM MGNLGYELDL
AILTKNEKKA VANQIKHYKK IRSVVQFGKL YRLINPEVGI NEVAVQYTYD NQVLVTYVRI
QSTIEMMETT VKLRGLDADA IYVLIETGQI FSGAELMYAG LTIDMPQGDY LSKQYYFIKK
