ID W2ZC27_PHYPR Unreviewed; 1142 AA.
AC W2ZC27;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=alpha-glucosidase {ECO:0000256|ARBA:ARBA00012741};
DE EC=3.2.1.20 {ECO:0000256|ARBA:ARBA00012741};
DE AltName: Full=Maltase {ECO:0000256|ARBA:ARBA00041343};
GN ORFNames=F442_09595 {ECO:0000313|EMBL:ETP43729.1};
OS Phytophthora parasitica P10297.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317064 {ECO:0000313|EMBL:ETP43729.1, ECO:0000313|Proteomes:UP000018948};
RN [1] {ECO:0000313|EMBL:ETP43729.1, ECO:0000313|Proteomes:UP000018948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P10297 {ECO:0000313|EMBL:ETP43729.1,
RC ECO:0000313|Proteomes:UP000018948};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P10297.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001657};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETP43729.1}.
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DR EMBL; ANIY01002014; ETP43729.1; -; Genomic_DNA.
DR AlphaFoldDB; W2ZC27; -.
DR EnsemblProtists; ETP43729; ETP43729; F442_09595.
DR Proteomes; UP000018948; Unassembled WGS sequence.
DR GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06602; GH31_MGAM_SI_GAA; 1.
DR CDD; cd14752; GH31_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR005085; CBM25.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR030459; Glyco_hydro_31_CS.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR PANTHER; PTHR22762:SF133; ALPHA-GLUCOSIDASE; 1.
DR Pfam; PF03423; CBM_25; 2.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SMART; SM01066; CBM_25; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS00707; GLYCOSYL_HYDROL_F31_2; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000018948}.
FT DOMAIN 90..174
FT /note="Carbohydrate binding module family 25"
FT /evidence="ECO:0000259|SMART:SM01066"
FT DOMAIN 197..280
FT /note="Carbohydrate binding module family 25"
FT /evidence="ECO:0000259|SMART:SM01066"
SQ SEQUENCE 1142 AA; 123925 MW; C7174C00A2C31EC8 CRC64;
MLQLPRGPST SAPRSPSLVT RICWRRNSVE LQRRQAPVSH SSICFLLSSK TMTLFTARLH
RSAAFIGCMA LVSNLLTSVT TAQTTVSTGG TSVHVLFQTD KWVTPNIHYK AGSGSWTTSP
GVAMSASNNS AYPSNDGWFQ FDVSSATSLE FVFNDGVGAV WDNNNNANYK VSVAGTYSVV
SKVSDFKTGD LVRPSDGTGY HILFQPITWA KPYMHFNAGS GWTTVPGYIM TPSTYAGKFS
AANGWYQYDI SSTSSVEITF NDGNGVWDSN LNANYIRTSP GTYAFVNQNT AAPTTSPSVQ
GYINGPGYSV TSASEDAGVL TINLAVNTAS TSTPYGSDLS ALVVTVTKTE KDSVRVKILD
KNSKRWEVPR DLFTAGSLGT DSTATSAATD PLYSFNYTQN PFTFKVVRKS DGYTLFDSSG
ISLVVKDQYL QVATALGSDL SVYGIGESTR DNFKMSSGDK QTLWARDQGS ATPIVNTYGS
HPFFLGINSA GQAHGVLLLN SNGMDVTMDS GHLVYQAIGG VLDFNIVVGP TPANVVSQYT
KLIGRPKLMP YWSYGFHQCR WGYGSVDALR TVVNKYKSSN LPLDVIWADI DYMKNFHDFT
LDPVNFPQAK MAAFMDEIHS SGQKFVPIID PGIPDDTNDY AYTKGLSMDI FIKDTSGKPY
LGQVWPGPTV FPDFFHPDAK SYWGEQIQLM YKSYNFDGLW IDMNELANFC PGTTCVRQSG
VTCPNTGSIS AITTCCLKCS GDGNKFDNPP FAINNVNSRD AIYNKGISTS ALQYGNIRQY
DTHNLYGITE SIVTNAVQEE LDNKRSFVLS RSTFPGSGAH VAHWTGDNAA TWNDLRWSVP
TILKFGLFGI PMVGADICGF SGASNMELCA RWTALGSFYP FARNHNNLES PAQETYVWPE
VATVGQKFIG MRYRLLPYIY TLGYHAHVGG LPIARPLLME FPTDTATYGI NHQFMLGNAL
LVTPVVNQGA TSVTGYYPAG VWYNIFDYSK ISSTGRSVTT TVTLYDMPVH IRGGTILAMH
QAALTSTAAR LTPFDILVAL PATGSANGDL YLDDGETISN PSATIVKFAA SAGTFTSTVE
KNDYAGAHSS LVNKVIVLGV TSSPSSVSLG SISKYDSATQ RLEISLSSVK QAIDTSFTIT
WK
//
