AGLU_CANTS
ID AGLU_CANTS Reviewed; 1070 AA.
AC P29064;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Alpha-glucosidase;
DE EC=3.2.1.20;
DE AltName: Full=Maltase;
DE Contains:
DE RecName: Full=Alpha-glucosidase subunit 1;
DE Contains:
DE RecName: Full=Alpha-glucosidase subunit 2;
DE Flags: Precursor;
OS Candida tsukubaensis (Yeast) (Pseudozyma tsukubaensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=5483;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 36-49 AND
RP 613-634.
RC STRAIN=CBS 6389;
RX PubMed=1761061; DOI=10.1111/j.1432-1033.1991.tb16420.x;
RA Kinsella B.T., Hogan S., Larkin A., Cantwell B.A.;
RT "Primary structure and processing of the Candida tsukubaensis alpha-
RT glucosidase. Homology with the rabbit intestinal sucrase-isomaltase complex
RT and human lysosomal alpha-glucosidase.";
RL Eur. J. Biochem. 202:657-664(1991).
CC -!- FUNCTION: Hydrolyzes a broad range of alpha-D-linked glucopyranosides,
CC including maltose (alpha-1,4), sucrose (alpha-1,2), isomaltose (alpha-
CC 1,6) and turanose (alpha-1,3).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR EMBL; X56024; CAA39501.1; -; Genomic_DNA.
DR PIR; S19686; S19686.
DR AlphaFoldDB; P29064; -.
DR SMR; P29064; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR CLAE; AGL31A_CANTS; -.
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;
KW Zymogen.
FT SIGNAL 1..35
FT /evidence="ECO:0000269|PubMed:1761061"
FT CHAIN 36..612
FT /note="Alpha-glucosidase subunit 1"
FT /id="PRO_0000018578"
FT CHAIN 613..1070
FT /note="Alpha-glucosidase subunit 2"
FT /id="PRO_0000018579"
FT ACT_SITE 526
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10066"
FT ACT_SITE 529
FT /evidence="ECO:0000250"
FT ACT_SITE 730
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 885
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 916
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 983
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 992
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1008
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1029
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1043
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1052
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1070 AA; 118631 MW; EE990FAA0770FA4B CRC64;
MRSIKAASLT PLLAALFTTL SSTLALPSSV WEHQLETNVL ALRDTNNNGS SSTISPSFDV
TKCPGYKLVG QPQQSQHGFT AQLSLAGDAC NAYGVDIANL TLSVVYEKQH QLHVHIYDTA
KQQYQLPNGL IFDRPGDNPA DIQNGSTADQ SDLVFHHTAE NGTQSGNGGW AFWIARKSSG
DVIFDTRASN IPTYNDGLSS VSSNTKRNTT AMPAHEMVFE NQYLQISSAL PTGANIYGLG
EYVTGSFRRN PDETLQPFFT LDAGTPVDSN MYGYHPIYTE ARRGSDGKLR THSVHLQNTA
GMDVLLRRGV IQYRAIGGTL DFRFFSGDQP ASSSSSSSGN DKAVATVKNS PNTAIQQYVN
FIGNPVIHPY WSYGFHLCRW GYNNVSETQA VIDAMRQNNI PLEVQWNDID YLQEFRDFTT
DPQRFPQKEF AAMIAKLKDN HQHYIPIIDM AIPKAPTNDT DVYYPGTRGD ELDVFIKNRN
GSQYIGEVWP GYTNFVDQQA ENAGKWWTEA IRNFSEIVDF SGIWLDMNEP SSFVIGNAAG
PETNLSNTPA YTAATSVAGW PQGYNNLTWG TSGNITVNGS YTYQQGPVQN NDGSKQRRSL
LLSRDEDVLV QRDINVNGGN GDKFGPEDPN YQYANSSQRY LSNPPYAIHN GIHISETPLN
VNLDKKTVAM EAVGVDGQRA FYDVHNLDGT LEEQHFYNAL RDIRPQERPF LISRSTYPGA
GKFTGHWLGD NYALWTILPG EEAYKAGAGM AQSIDGVLQF QIFGIHLIGA DICGFNRNSD
EELCNRWMML GAFLPFMRNH NTIGAIAQEP FRWDSVANAS RIAINKRYEI LPSLYSHMAQ
SAESGEPAVR ALWYEFDEVF EQTKDYAHQF LFGDDLLVSP VLEPNVTQIK ALFPNAGGKW
RNVFSYEALD VEYNKNVTVD AALSTINVHL RPGKVLLTHS KPAYTVYETA QSPYGLIVNL
NDQGEAKQTF YLDDGMTPAP TPNSTLTVSA GNNSVNGSIE GEYKAQQNLT YVVVLDVKQK
PTQVMMGGNK TEFSWDQQKT LLNVTGLNAD LNGSGRFRGL RLELSLLCED
