ID D8Q2K0_SCHCM Unreviewed; 470 AA.
AC D8Q2K0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 56.
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};
DE Flags: Fragment;
GN ORFNames=SCHCODRAFT_107514 {ECO:0000313|EMBL:EFI98134.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFI98134.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
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; GL377305; EFI98134.1; -; Genomic_DNA.
DR RefSeq; XP_003033037.1; XM_003032991.1.
DR AlphaFoldDB; D8Q2K0; -.
DR STRING; 578458.D8Q2K0; -.
DR GeneID; 9592724; -.
DR KEGG; scm:SCHCO_02676633; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02676633; -.
DR eggNOG; KOG2212; Eukaryota.
DR HOGENOM; CLU_013336_0_0_1; -.
DR InParanoid; D8Q2K0; -.
DR OMA; FRYAYDL; -.
DR OrthoDB; 3249969at2759; -.
DR Proteomes; UP000007431; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
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; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007431};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..470
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003120530"
FT DOMAIN 32..376
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 385..469
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT NON_TER 470
FT /evidence="ECO:0000313|EMBL:EFI98134.1"
SQ SEQUENCE 470 AA; 50067 MW; 66A94CBDE64336F0 CRC64;
MSLRSALLAS ALIGARALPA PHGARAPSSD NKVIIQIFEW NWDSIAQECT DFIGPAGYGF
VQVSPPQETI SGDQWWTDYQ PVSYILQGKR GDRDGFAAMV EACHDAGVGV IADTIWNHMA
GVDSGTGTAG SSFTHYDYPG IYQTQDFHHC GLESGDDIVN YSNREEVQTC ELVNLADLAT
DTDYVRGKLA DYANDLISLG VDGLRLDASK HIPTDDIAAI ISRLNSSVYI TQEVIYGDGE
PITPAEYVQN GDVQEFRYTH TIQDAFTNSG LDQLQDLDSK GWVAGSSANV FVANHDTERG
GDSLNYNSPN NIYTTAMIFS LAHPYGTPSI LSSFEFSNSD DGAPNGNAGT CSDDGGASGW
ICQHRWPAVR NMVAFRNEVG DAELTDWVSP QGSQIAFGRG SAGYVAINNA DSEWSTTFST
SLADGSYCDV ISGDASDGSC SGNTITVSGG SFDATVPARS ALAIHTGATV
//
