AGLU_ASPNG
ID AGLU_ASPNG Reviewed; 985 AA.
AC P56526; O13451;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Alpha-glucosidase;
DE EC=3.2.1.20;
DE AltName: Full=Maltase;
DE Flags: Precursor;
GN Name=aglA;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GN-3;
RX PubMed=9165762; DOI=10.1016/s0168-1656(97)01664-7;
RA Nakamura A., Nishimura I., Yokoyama A., Lee D.-G., Hidaka M., Masaki H.,
RA Kimura A., Chiba S., Uozumi T.;
RT "Cloning and sequencing of an alpha-glucosidase gene from Aspergillus niger
RT and its expression in A. nidulans.";
RL J. Biotechnol. 53:75-84(1997).
RN [2]
RP PROTEIN SEQUENCE OF 26-252 AND 267-985, AND GLYCOSYLATION AT THR-36;
RP ASN-124; ASN-143; ASN-218; ASN-347; ASN-422; ASN-506; ASN-534; SER-545;
RP SER-550; THR-559; SER-560; THR-561; SER-562; THR-571; ASN-601; ASN-623;
RP ASN-835; ASN-881; SER-895; ASN-899; ASN-957 AND ASN-970.
RC STRAIN=GN-8;
RX PubMed=1368849; DOI=10.1271/bbb.56.1368;
RA Kimura A., Takata M., Sakai O., Matsui H., Takai N., Takayanagi T.,
RA Nishimua I., Uozumi T., Chiba S.;
RT "Complete amino acid sequence of crystalline alpha-glucosidase from
RT Aspergillus niger.";
RL Biosci. Biotechnol. Biochem. 56:1368-1370(1992).
CC -!- FUNCTION: Hydrolyzes malto-oligosaccharides, but has a low activity
CC toward soluble starch.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC -!- PTM: The O-linked saccharide is not identified, but is probably
CC mannose. {ECO:0000269|PubMed:1368849}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR EMBL; D45356; BAA23616.1; -; Genomic_DNA.
DR PIR; JC1199; JC1199.
DR PIR; JC1200; JC1200.
DR PIR; JC5561; JC5561.
DR AlphaFoldDB; P56526; -.
DR SMR; P56526; -.
DR STRING; 5061.CADANGAP00004308; -.
DR BindingDB; P56526; -.
DR ChEMBL; CHEMBL3435; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR CLAE; AGL31A_ASPNG; -.
DR GlyConnect; 43; 7 N-Linked glycans.
DR iPTMnet; P56526; -.
DR VEuPathDB; FungiDB:An04g06920; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1146704; -.
DR VEuPathDB; FungiDB:ATCC64974_81710; -.
DR VEuPathDB; FungiDB:M747DRAFT_360506; -.
DR eggNOG; KOG1065; Eukaryota.
DR BRENDA; 3.2.1.20; 518.
DR GO; GO:0004558; F:alpha-1,4-glucosidase activity; IDA:AspGD.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.40.1180; -; 2.
DR InterPro; IPR031727; Gal_mutarotase_N.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR Pfam; PF16863; NtCtMGAM_N; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:1368849"
FT CHAIN 26..985
FT /note="Alpha-glucosidase"
FT /id="PRO_0000018576"
FT ACT_SITE 490
FT /note="Nucleophile"
FT ACT_SITE 493
FT /evidence="ECO:0000250"
FT ACT_SITE 660
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 36
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000305|PubMed:1368849"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1368849"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1368849"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1368849"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1368849"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1368849"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1368849"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1368849"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 545
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000305|PubMed:1368849"
FT CARBOHYD 550
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000305|PubMed:1368849"
FT CARBOHYD 559
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000305|PubMed:1368849"
FT CARBOHYD 560
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000305|PubMed:1368849"
FT CARBOHYD 561
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000305|PubMed:1368849"
FT CARBOHYD 562
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000305|PubMed:1368849"
FT CARBOHYD 571
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000305|PubMed:1368849"
FT CARBOHYD 601
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1368849"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1368849"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1368849"
FT CARBOHYD 881
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1368849"
FT CARBOHYD 895
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000305|PubMed:1368849"
FT CARBOHYD 899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1368849"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1368849"
FT CARBOHYD 970
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1368849"
FT VARIANT 27..28
FT /note="TT -> LL (in strain: GN-8)"
FT VARIANT 42
FT /note="D -> A (in strain: GN-8)"
FT VARIANT 929
FT /note="N -> M (in strain: GN-8)"
SQ SEQUENCE 985 AA; 108913 MW; 9A18772AEB2E0927 CRC64;
MVKLTHLLAR AWLVPLAYGA SQSLLSTTAP SQPQFTIPAS ADVGAQLIAN IDDPQAADAQ
SVCPGYKASK VQHNSRGFTA SLQLAGRPCN VYGTDVESLT LSVEYQDSDR LNIQILPTHV
DSTNASWYFL SENLVPRPKA SLNASVSQSD LFVSWSNEPS FNFKVIRKAT GDALFSTEGT
VLVYENQFIE FVTALPEEYN LYGLGEHITQ FRLQRNANLT IYPSDDGTPI DQNLYGQHPF
YLDTRYYKGD RQNGSYIPVK SSEADASQDY ISLSHGVFLR NSHGLEILLR SQKLIWRTLG
GGIDLTFYSG PAPADVTRQY LTSTVGLPAM QQYNTLGFHQ CRWGYNNWSD LADVVANFEK
FEIPLEYIWT DIDYMHGYRN FDNDQHRFSY SEGDEFLSKL HESGRYYVPI VDAALYIPNP
ENASDAYATY DRGAADDVFL KNPDGSLYIG AVWPGYTVFP DWHHPKAVDF WANELVIWSK
KVAFDGVWYD MSEVSSFCVG SCGTGNLTLN PAHPSFLLPG EPGDIIYDYP EAFNITNATE
AASASAGASS QAAATATTTS TSVSYLRTTP TPGVRNVEHP PYVINHDQEG HDLSVHAVSP
NATHVDGVEE YDVHGLYGHQ GLNATYQGLL EVWSHKRRPF IIGRSTFAGS GKWAGHWGGD
NYSKWWSMYY SISQALSFSL FGIPMFGADT CGFNGNSDEE LCNRWMQLSA FFPFYRNHNE
LSTIPQEPYR WASVIEATKS AMRIRYAILP YFYTLFDLAH TTGSTVMRAL SWEFPNDPTL
AAVETQFMVG PAIMVVPVLE PLVNTVKGVF PGVGHGEVWY DWYTQAAVDA KPGVNTTISA
PLGHIPVYVR GGNILPMQEP ALTTREARQT PWALLAALGS NGTASGQLYL DDGESIYPNA
TLHVDFTASR SSLRSSAQGR WKERNPLANV TVLGVNKEPS AVTLNGQAVF PGSVTYNSTS
QVLFVGGLQN LTKGGAWAEN WVLEW
