ID G4YVX3_PHYSP Unreviewed; 712 AA.
AC G4YVX3;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN ORFNames=PHYSODRAFT_556403 {ECO:0000313|EMBL:EGZ23727.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ23727.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ23727.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ23727.1,
RC ECO:0000313|Proteomes:UP000002640};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548,
CC ECO:0000256|RuleBase:RU361134};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; JH159152; EGZ23727.1; -; Genomic_DNA.
DR RefSeq; XP_009519015.1; XM_009520720.1.
DR AlphaFoldDB; G4YVX3; -.
DR STRING; 1094619.G4YVX3; -.
DR EnsemblProtists; EGZ23727; EGZ23727; PHYSODRAFT_556403.
DR GeneID; 20663170; -.
DR KEGG; psoj:PHYSODRAFT_556403; -.
DR InParanoid; G4YVX3; -.
DR OMA; PVNFVWQ; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR005085; CBM25.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF03423; CBM_25; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Reference proteome {ECO:0000313|Proteomes:UP000002640}.
FT DOMAIN 252..696
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 65..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 712 AA; 77134 MW; F2BE2B9B576B726D CRC64;
MTASTDPTYP ASVGWFQYDV AVPQASLEFV FNNGNGVWDN NKNANYEATS AGKWIVMSTV
SVPPATTTTT TPTTAPAPPT ATPKPTTASP TPTSTAAPSP TTSAPTPSGS CYNYNGQDSC
SSSTQTELPA SDDQRKWQTP PRNASGWSTD YQDYRSLTGY AHVVYGAART SATVTVRTFL
RVASATCSFT FNGVKSTSAT YQVTNALKDD LIIVVTCTDG TDTWTLELDP VNFVWQNNAV
NQPSGMKGGQ KGAIVDLFGW PYDDIAQECS DFLGKASYMG VKINPPQESV LTDAWPQNGQ
RNPWYFVYQP VSYRLYSRLG TRAQLRSMIQ TCRANGVRVY ADAVVNHMSG GGNDVLSHRY
SSGGSCVTWG AKSSAKHSPY YTHSYTYGVN EYTKARPALE FPAVPYGPSD FHCERTMSSW
TDPLQLETGW LTGLTDLNTE KTYVRERIAQ YFVDLLGIGF SGLRLDALKH IGPVDAGAIY
GLLNTFMGGS LPDDFISWGE VILGGEASLL ACNADSGYNF YKGLDAQYAA NGISSTDIAK
LKIWSSDYPK EFPICGSWIL PSSRFVIQND DHDQQNDGSS SRDMGDAGSV LIKDKDVARH
RSFEVKLFSR TDADWQIKVV LSSYTWFSNG AAGFPDGYSD CSGFDSSQGQ KCTASVPYEK
AFRAGSCGYT VEGFAGGKYT RVHRDLSIVN AMRSWIGLSS VTLAGLGISG SC
//
