ID A0A094DMV8_9PEZI Unreviewed; 494 AA.
AC A0A094DMV8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=V497_03378 {ECO:0000313|EMBL:KFY60780.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY60780.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY60780.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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 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}.
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:KFY60780.1}.
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DR EMBL; JPJZ01000780; KFY60780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DMV8; -.
DR STRING; 1420910.A0A094DMV8; -.
DR HOGENOM; CLU_006462_7_2_1; -.
DR OrthoDB; 3249969at2759; -.
DR Proteomes; UP000029268; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
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; IPR006046; Alpha_amylase.
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 PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR001024-3};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001024-4};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001024-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..494
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001900456"
FT DOMAIN 38..391
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 229
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT ACT_SITE 253
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT SITE 318
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-2"
FT DISULFID 54..60
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 173..186
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
SQ SEQUENCE 494 AA; 53442 MW; CB01BAE79D978AC2 CRC64;
MSLRSITQVV EMLLITTSFL SIAAAKTAAE WRELSIYQVL TDRFATTDGS SPSCAITDYC
GGTWKGLENR LDYIQGMGFQ AVWISPVVHN IDGDTPAGYA YHGYWADDPF TLNDHFGTTD
DLKSLSQALH GRGMSLMIDV VINHFGASQD SGSVNYSAYP SPFNNAGAFH SPCAIDYNDQ
ASIENCWVVT TPAPSLPDIN SEDATIFTAL VDSVVDLVSN YSIDGIRLDT AKHVPQEYLT
QFQEAVGVFV IGEALDGDPA YVSGYQGPLD SAINYPLWYP LITAFMGGNF DSLATMISTE
ATSFSDVNAL TNFLDNHDQP RIASQAGDDE VKDKNAVTFL MFTSGIPMVY YGFEQRFTGA
ADPDNRETLW TSSYDTTTTL YQYIAQLHEI RGIASNVTDK ATYFSSNVAV LGTSSEYMAL
ERGPVVVVVS NVGAAGASDG FSITGSQFSS GDTVVDLLDC TTATVDESGV FISQSNNGEA
RIWIRAENKD SLCS
//
