AGALG_ASPTN
ID AGALG_ASPTN Reviewed; 725 AA.
AC Q0CEF5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Probable alpha-galactosidase G;
DE EC=3.2.1.22;
DE AltName: Full=Melibiase G;
GN Name=aglG; ORFNames=ATEG_07929;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes a variety of simple alpha-D-galactoside as well as
CC more complex molecules such as oligosaccharides and polysaccharides.
CC {ECO:0000250}.
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; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 36 family. {ECO:0000305}.
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DR EMBL; CH476604; EAU32191.1; -; Genomic_DNA.
DR RefSeq; XP_001216550.1; XM_001216550.1.
DR AlphaFoldDB; Q0CEF5; -.
DR SMR; Q0CEF5; -.
DR STRING; 341663.Q0CEF5; -.
DR EnsemblFungi; EAU32191; EAU32191; ATEG_07929.
DR GeneID; 4322588; -.
DR VEuPathDB; FungiDB:ATEG_07929; -.
DR eggNOG; ENOG502QWG1; Eukaryota.
DR HOGENOM; CLU_009640_2_1_1; -.
DR OMA; FNSWEAT; -.
DR OrthoDB; 472260at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase; Magnesium;
KW NAD; Polysaccharide degradation; Reference proteome; Secreted.
FT CHAIN 1..725
FT /note="Probable alpha-galactosidase G"
FT /id="PRO_0000395068"
FT ACT_SITE 484
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT ACT_SITE 546
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 725 AA; 80322 MW; FB549C2032C1F01F CRC64;
MTIENGIAKA IYVDGTKFVL NGRHVSYCFH VDDETGDLRT DHFGGRVTGA IPVDPSPVVD
GWTGMPDRVR REFPDQGRGD FRIPALRIRQ AEGHTVSALK YQSYTLLHGK PDLPGLPATF
GTEKDVSTLV VHLRDEYSSV TADLIYSVFP EYNAIVRSVS ITNNGFQPIS IEALASFSTD
LPYEDLEMIS LRGDWAREAH RMRRKVEYGT QGFGSTTGFS SHLHNPFLAL AHPSTTESQG
EAWGFSLVYT GSFEVNVEKG SQGLTRAVLG FHPNQLSWPL SPGETLTSPE CVAVYSNHGL
GGMSRSLHRL FRDHLIKSKF ATANRPVLLN SWEGLYFDID ETSMIRIAKE SAALGVKLLV
MDDGWFGKDY PRTSDAAGLG DWVPNPARFP NGLAPMVDQI TSLKVANSSA NLLFGIWVEP
EMVNPDSALY REHPEWALHA GSYPRTEQRN QLVLNLALLE VQEFIINFMT DLLSSAKISY
VKWDLNRGIN ETSAPKATHA YMLGMYKVFD TLTSRFPDVL WEGCAAGGGR FDPGILQYFP
QIWTSDDSDA VERIFIQMGS SLAYPASAMG AHISAVPNHQ TGRTTPLSLR AHVAMMGGSF
GLELDPSQVS AEEKALIPEL IALAEKVNPI VLTGDMWRLS LPEESNWPAV QFISQDQSQV
VLFYFQLSPN VNHSMPRVRL QGLDEDAMYR VDGAGPYSGA MLMNLGLQYS FRTEYGSRVV
FLEKQ