AMYG_CANAL
ID AMYG_CANAL Reviewed; 946 AA.
AC O74254; A0A1D8PEU6; Q5AP64; Q5APQ9;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Glucoamylase 1;
DE EC=3.2.1.3;
DE AltName: Full=1,4-alpha-D-glucan glucohydrolase;
DE AltName: Full=Glucan 1,4-alpha-glucosidase;
DE Flags: Precursor;
GN Name=GAM1; Synonyms=GCA1; OrderedLocusNames=CAALFM_C110290WA;
GN ORFNames=CaO19.12365, CaO19.4899;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 193-213; 776-792
RP AND 817-835.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=10520161; DOI=10.1046/j.1365-280x.1999.00244.x;
RA Sturtevant J., Dixon F., Wadsworth E., Latge J.-P., Zhao X.-J.,
RA Calderone R.;
RT "Identification and cloning of GCA1, a gene that encodes a cell surface
RT glucoamylase from Candida albicans.";
RL Med. Mycol. 37:357-366(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues
CC successively from non-reducing ends of the chains with release of
CC beta-D-glucose.; EC=3.2.1.3; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10066};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Peripheral
CC membrane protein.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR EMBL; AF082188; AAC31968.1; -; Genomic_DNA.
DR EMBL; CP017623; AOW26659.1; -; Genomic_DNA.
DR RefSeq; XP_723581.2; XM_718488.2.
DR AlphaFoldDB; O74254; -.
DR SMR; O74254; -.
DR BioGRID; 1217997; 1.
DR STRING; 237561.O74254; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR PRIDE; O74254; -.
DR GeneID; 3634903; -.
DR KEGG; cal:CAALFM_C110290WA; -.
DR CGD; CAL0000192588; GCA1.
DR VEuPathDB; FungiDB:C1_10290W_A; -.
DR eggNOG; KOG1065; Eukaryota.
DR HOGENOM; CLU_000631_11_0_1; -.
DR InParanoid; O74254; -.
DR OrthoDB; 151244at2759; -.
DR PRO; PR:O74254; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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 Carbohydrate metabolism; Cell wall; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..946
FT /note="Glucoamylase 1"
FT /id="PRO_0000018585"
FT REGION 517..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 462
FT /evidence="ECO:0000250"
FT ACT_SITE 465
FT /evidence="ECO:0000250"
FT ACT_SITE 628
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 570
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 772
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 912
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 242
FT /note="N -> D (in Ref. 1; AAC31968)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="A -> G (in Ref. 1; AAC31968)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="N -> D (in Ref. 1; AAC31968)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="G -> D (in Ref. 1; AAC31968)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="T -> A (in Ref. 1; AAC31968)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="N -> D (in Ref. 1; AAC31968)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="G -> A (in Ref. 1; AAC31968)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="N -> K (in Ref. 1; AAC31968)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="V -> I (in Ref. 1; AAC31968)"
FT /evidence="ECO:0000305"
FT CONFLICT 918
FT /note="N -> K (in Ref. 1; AAC31968)"
FT /evidence="ECO:0000305"
FT CONFLICT 943..944
FT /note="SI -> TL (in Ref. 1; AAC31968)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 946 AA; 105717 MW; D8A3D1BB2B7DD2B4 CRC64;
MKLLSKVFVT ALGLTSIVNA APTSSSSAEE AQKTVPVELS IGVKQLPNIH NDSAVDANAV
AKGYSLVNVS LTARGLTGIL KLKEATNIYG YDFEYLNLSV EYQSDTRLNV HIEPTDLTDV
FVLPEELVVK PKLEGDAKTF NFENSDLVFE YDEEDFGFEV LRSSTREVLF STKGNPLVFS
NQFIQFNTTL PKGHSITGLG ESIHGSLNEP GVVKTLYAND IADPIDGNIY GVHPVYYDQR
YNTNTTHAVY WRTSAIQEVV VGETSLTWRA LSGVIDLYFF SGPDPKDVIQ QYVSEIGLPA
MQPYWALGYH QCRWGYDTVE SLETVVENFK KFDIPLETIW SDIDYMDGYK DFTNDPYRFP
TDKFRKFLDD LHNNSQHYVP IFDAAIYVPN PNNATDNDYE PFHLGNESDV FLKNPDGSLY
IGAVWPGYTV FPDFLANNTQ EYWNKMFKDW YERIPFDGIW TDMNEVSSFC VGSCGTGRYF
DNPVHPPFEV GYSGSDYPLG FDKSNASEWK SISEAAAATK TTTTTSSSTS TSIDGKNTLA
PGKGNINYPP YAINNNQGDH DLATHAISPN ATHADGTVEY DIHNIYGLIQ ERAIYEALLE
IHPNKRPFII GRSSFAGSGK YMGHWGGDNY ADYYMMYFSI PQALSMGLSG IPFFGVDACG
FNGNTDMELC SRWMQLASFF PFYRNHNVLG AIPQEPYVWE GVMNATKTSI NVRYSLLPYY
YTLLHESHVT GIPIMRAFNW QFPYSKELAG VDTQFFVGDA LLVTPVLEPG VNHTKGVFPG
ENAVYYDFYT HKKQKFTAGK NETLAAPLGH IPLHIKGGNI IPTQEPGYTT TESRKNPFGL
LVALDAEGTA SGKLYLDDGE SVDVEEALYV DFVASKNKLV ASVFGEYEVR QPLANVTILG
VDSEPKKVLF NNETVSHNYE NGAVYLTDLE KFTKEGAFAE EFSIQW
