AGALC_ASPTN
ID AGALC_ASPTN Reviewed; 747 AA.
AC Q0CVH2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Probable alpha-galactosidase C;
DE EC=3.2.1.22;
DE AltName: Full=Melibiase C;
DE Flags: Precursor;
GN Name=aglC; ORFNames=ATEG_02312;
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; CH476596; EAU37274.1; -; Genomic_DNA.
DR RefSeq; XP_001211490.1; XM_001211490.1.
DR AlphaFoldDB; Q0CVH2; -.
DR SMR; Q0CVH2; -.
DR STRING; 341663.Q0CVH2; -.
DR EnsemblFungi; EAU37274; EAU37274; ATEG_02312.
DR GeneID; 4316651; -.
DR VEuPathDB; FungiDB:ATEG_02312; -.
DR eggNOG; ENOG502QWG1; Eukaryota.
DR HOGENOM; CLU_009640_2_1_1; -.
DR OMA; WEGIYFD; -.
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; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..747
FT /note="Probable alpha-galactosidase C"
FT /id="PRO_0000395066"
FT ACT_SITE 507
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT ACT_SITE 569
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 747 AA; 82573 MW; AA81EF8F9ABD51C6 CRC64;
MVAFMNSATF VAGLFTLWSR PIWATPASNT NAVVVNGTAF TLNGDHVSYR FHVDDATGDL
FSDHFGPRVS GNFPTEIVSQ VNGWVNTIGR VRREFPDQGR GDFRIPAIRI RQTAGYTVSE
LLYRSHTVIP GKPALPGLPA TFGSEEDVTT LVVHLYDEIS EVAADLSYSI FPKYDAVVRS
VNVTNQGAGN ITIETLASLS VDFPYEDLDM VYLRGDWARE AHSERRKVEY GTQGFDSSAG
YSSHLHNPFL AIMNPATTES QGETWGFSLV YSGSFAVNVE RGSQGFTRAL LGLNPGQLSW
VLRPGESLVS PECVAVYSAD GIGGMSRLLH RLYRNHLIKS KFAVSDRPVL LNSWEGLGFN
YNETTVYQLA TEAAELGVKL FVLDDGWFGD KYPRTADNAG LGDWVPNPDR FPHGLPHEVD
RITALHPGND TSTNLRFGLW FEPEMVNPNS SLYHQHPDWA LHAGSYPRTL TRNQLVLNMA
LPEVQDYVIK SVSDILDSAD ISYVKWDNNR GIHETPSPST DHQYMLGMYR VFDNLTTKYP
NVLWEGCASG GGRFDPGVLQ YFPQIWTSDD TDALERITIQ MGTSLAYPPS AMGAHLSAVP
NQQTGRTLPI TFRAHVAMMG GSFGLELNPA HMPDDERDAV PGLIALAERV NPIVLTGDMY
RLSPHDSQWP AVLFISPDGE QAVLFYFQTS PRVDNSIPRV KMQGLDPQAV YSVDGDAEYS
GATLMNVGLQ FPFDSDVGSK VVFFQRL
