ID   AGAL_SACS2              Reviewed;         648 AA.
AC   Q97U94;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Alpha-galactosidase;
DE            Short=Alpha-Gal;
DE            EC=3.2.1.22;
GN   Name=galS; OrderedLocusNames=SSO3127;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   MUTAGENESIS OF ASP-367 AND ASP-425, AND CHARACTERIZATION.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=16547025; DOI=10.1128/jb.188.7.2392-2399.2006;
RA   Brouns S.J.J., Smits N., Wu H., Snijders A.P.L., Wright P.C., de Vos W.M.,
RA   van der Oost J.;
RT   "Identification of a novel alpha-galactosidase from the hyperthermophilic
RT   archaeon Sulfolobus solfataricus.";
RL   J. Bacteriol. 188:2392-2399(2006).
CC   -!- FUNCTION: Involved in the degradation of various alpha-linked
CC       galactosides such as raffinose, stachyose and melibiose.
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   -!- ACTIVITY REGULATION: Completely inhibited by most divalent metal
CC       cations, however magnesium and molybdene have no effect.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.08 mM for para-nitrophenol-alpha-D-galactopyranoside;
CC         KM=37.4 mM for para-nitrophenol-beta-L-arabinopyranoside;
CC       pH dependence:
CC         Optimum pH is 5.0.;
CC       Temperature dependence:
CC         Optimum temperature is 90 degrees Celsius.;
CC   -!- SUBUNIT: Trimer. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 36 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK43227.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE006641; AAK43227.1; ALT_INIT; Genomic_DNA.
DR   PIR; D90496; D90496.
DR   AlphaFoldDB; Q97U94; -.
DR   SMR; Q97U94; -.
DR   STRING; 273057.SSO3127; -.
DR   CAZy; GH36; Glycoside Hydrolase Family 36.
DR   EnsemblBacteria; AAK43227; AAK43227; SSO3127.
DR   KEGG; sso:SSO3127; -.
DR   PATRIC; fig|273057.12.peg.3232; -.
DR   eggNOG; arCOG06049; Archaea.
DR   HOGENOM; CLU_415982_0_0_2; -.
DR   InParanoid; Q97U94; -.
DR   OMA; AYPDYDM; -.
DR   BRENDA; 3.2.1.22; 6163.
DR   SABIO-RK; Q97U94; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR008811; Glycosyl_hydrolases_36.
DR   PANTHER; PTHR31268; PTHR31268; 1.
DR   Pfam; PF05691; Raffinose_syn; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..648
FT                   /note="Alpha-galactosidase"
FT                   /id="PRO_0000232659"
FT   ACT_SITE        367
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         367
FT                   /note="D->G: Hydrolase activity is below detection limit."
FT                   /evidence="ECO:0000269|PubMed:16547025"
FT   MUTAGEN         425
FT                   /note="D->G: Slightly increase of hydrolasee activity."
FT                   /evidence="ECO:0000269|PubMed:16547025"
SQ   SEQUENCE   648 AA;  74567 MW;  4263C97145745121 CRC64;
     MIWIEDENGN KYQCDSNGNC ENLAIVKVNT KEYNNDGKIY SIEGKSFVKL SKFPITLKLN
     LKADQILSLT TQQIYSEVYG KAFTYYNQLA IDMEPVTEPP KELKYDIKSL DHEKYIRTYP
     CWLYPVFNNI PDYTVFALVK SGNSYEAFFT LSNNYVTAYL FGDSVRLYTG FNTDEIKRSY
     FLSIGTSDNP YKAIENAINI ASKETFTFKL RKEKGFPDKV MNGLGWCSWN AFLTKDLNEE
     NLIKVVKGII ERGLRLNWVI IDDGWQDQNN DRAIRSLNPD NKKFPNGFKN TVRAIKSLGV
     KYVGLWHAIN AHWGGMSQEL MKSLNVNGYF TNFLNSYVPS PNLEDAIGFY KAFDGNILRD
     FDLVKVDNQW VIHAIYDSFP IGLASRNIQI ALQYSVGKDV INCMSMNPEN YCNYFYSNVM
     RNSIDYVPFW KDGTKLHIMF NAYNSLLTSH IVYPDYDMFM SYDPYAKVHL VARVFSGGPI
     YITDRHPERT NIELLRMAVL PNGEVIRVDE PALITEDLLF KDPLRERVLL KLKGKVKGYN
     AIAFFNLNSG EVEEEYNNNE DYYYYKVFSG EFGVGKFNVK LRELDAEVVI TFPKSNRVIG
     LREYILPPFT VIVSDNVVIP KADGTLLYVK DTELNEVKAR EGIPVTIE