ID A0A0C9SY79_PAXIN Unreviewed; 510 AA.
AC A0A0C9SY79;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=PAXINDRAFT_115611 {ECO:0000313|EMBL:KIJ14854.1};
OS Paxillus involutus ATCC 200175.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Paxilineae; Paxillaceae; Paxillus.
OX NCBI_TaxID=664439 {ECO:0000313|EMBL:KIJ14854.1, ECO:0000313|Proteomes:UP000053647};
RN [1] {ECO:0000313|EMBL:KIJ14854.1, ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|EMBL:KIJ14854.1,
RC ECO:0000313|Proteomes:UP000053647};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200175 {ECO:0000313|Proteomes:UP000053647};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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DR EMBL; KN819340; KIJ14854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9SY79; -.
DR HOGENOM; CLU_006462_7_2_1; -.
DR OrthoDB; 3249969at2759; -.
DR Proteomes; UP000053647; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR CDD; cd11319; AmyAc_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013777; A-amylase-like.
DR InterPro; IPR015340; A_amylase_C_dom.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF09260; A_amylase_dom_C; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001024-4};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000053647};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..510
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002213339"
FT DOMAIN 34..409
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT SITE 337
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-2"
FT DISULFID 55..63
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 189..203
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
SQ SEQUENCE 510 AA; 56949 MW; AA13BFDA95541A6F CRC64;
MLYSVLFLLT FGGFFCLESS AADAQQWRSR SIYQVMTDRF ALQDVSDGTA YNMPCNTSAL
QYCGGTWRGI IDHLDYIQGM GFDAIWISPP FANVEGPTPL GEAYHGYWPQ DLSSLNAHFG
TVNDLRNLSA SLHSRGMYLM LDIVVNHMVS QRPINITAVQ LATANTTVVI KNTTEMYPFE
DLSDFHDLCW IMDYSNQTEV EQCWLGDESM PWADVNTEDP EVVGTLNGWI TDVISDFGVD
GLRLSTVKYV SRDFWRSFTA QAGIFTMGEV FSVGANYTSP YTEVMDAVID YPTWFELVPA
FMSPQGDFDA LKNIVKQSQD LYTSGAFMTG SFLENHDQPR FGSLTNDTAL QANAMVWPFI
HDGIPILYYG QEQGLSGGES PNNQEALWGT RYDTEHPHYI TVTSLNQARK AAIKSEQYFL
TTPMQFLDAN EDNTLVVSKP PMLALLTNVG SQPTTSVRWN VTHPVFKSRE QLVDILTCRS
YISGENGGVS IQSGEGMPKV SLAMSLQEMI
//
