AGALC_ASPNG
ID AGALC_ASPNG Reviewed; 747 AA.
AC Q9UUZ4;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Alpha-galactosidase C;
DE EC=3.2.1.22;
DE AltName: Full=Melibiase;
DE Flags: Precursor;
GN Name=aglC {ECO:0000303|PubMed:11358516};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX PubMed=11358516; DOI=10.1046/j.1432-1327.2001.02188.x;
RA Ademark P., de Vries R.P., Haegglund P., Staalbrand H., Visser J.;
RT "Cloning and characterization of Aspergillus niger genes encoding an alpha-
RT galactosidase and a beta-mannosidase involved in galactomannan
RT degradation.";
RL Eur. J. Biochem. 268:2982-2990(2001).
CC -!- FUNCTION: Involved in galactomannan degradation.
CC {ECO:0000269|PubMed:11358516}.
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:0000269|PubMed:11358516};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P27756};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:P27756};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P27756}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 36 family.
CC {ECO:0000250|UniProtKB:P27756}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ251873; CAB63901.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9UUZ4; -.
DR SMR; Q9UUZ4; -.
DR STRING; 5061.CADANGAP00007429; -.
DR BindingDB; Q9UUZ4; -.
DR ChEMBL; CHEMBL3936; -.
DR DrugCentral; Q9UUZ4; -.
DR CAZy; GH36; Glycoside Hydrolase Family 36.
DR CLAE; MEL36C_ASPNG; -.
DR VEuPathDB; FungiDB:An09g00260; -.
DR VEuPathDB; FungiDB:An09g00270; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1098926; -.
DR VEuPathDB; FungiDB:ATCC64974_6090; -.
DR VEuPathDB; FungiDB:M747DRAFT_289615; -.
DR eggNOG; ENOG502QWG1; Eukaryota.
DR GO; GO:0004557; F:alpha-galactosidase activity; IDA:UniProtKB.
DR GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016052; P:carbohydrate catabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Glycoprotein; Glycosidase; Hydrolase; Magnesium; NAD; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..747
FT /note="Alpha-galactosidase C"
FT /id="PRO_0000001023"
FT ACT_SITE 508
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT ACT_SITE 570
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9ALJ4"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
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 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 747 AA; 81859 MW; 9429DAA59274ED00 CRC64;
MIGSSHAVVA LGLFTLYGHS AAAPAIGASN SQTIVTNGTS FALNGDNVSY RFHVNSSTGD
LISDHFGGVV SGTIPSPVEP AVNGWVGMPG RIRREFPDQG RGDFRIPAVR IRESAGYTVS
DLQYVSHEVI EGKYALPGLP ATFGDAQDAT TLVVHLYDNY SSVAADLSYS IFPKYDAIVR
SVNVTNQGPG NITIEALASI SIDFPYEDLD MVSLRGDWAR EANVQRSKVQ YGVQGFGSST
GYSSHLHNPF LAIVDPATTE SQGEAWGFNL VYTGSFSAQV EKGSQGFTRA LLGFNPDQLS
WNLGPGETLT SPECVAVYSD KGLGSVSRKF HRLYRNHLMK SKFATSDRPV LLNSWEGVYF
DYNQSSIETL AEESAALGVH LFVMDDGWFG DKYPRVSDNA GLGDWMPNPA RFPDGLTPVV
QDITNLTVNG TESTKLRFGI WVEPEMVNPN STLYHEHPEW ALHAGPYPRT ERRNQLVLNL
ALPAVQDFII DFMTNLLQDT GISYVKWDNN RGIHETPSPS TDHQYMLGLY RVFDTLTTRF
PDVLWEGCAS GGGRFDAGML QYVPQIWTSD NTDAIDRITI QFGTSLAYPP SAMGAHLSAV
PNAQTGRTVP FTFRAHVAMM GGSFGLELDP ATVEGDEIVP ELLALAEKVN PIILNGDLYR
LRLPQDSQWP AALFVSQDGA QAVLFYFQVQ PNVNHAVPWV RLQGLDPKAD YTVDGDQTYS
GATLMNLGLQ YSFDTEYGSK VVFLERQ
