ID B6H8T0_PENRW Unreviewed; 547 AA.
AC B6H8T0;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=Pc16g06140 {ECO:0000313|EMBL:CAP93284.1}, PCH_Pc16g06140
GN {ECO:0000313|EMBL:CAP93284.1};
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP93284.1, ECO:0000313|Proteomes:UP000000724};
RN [1] {ECO:0000313|EMBL:CAP93284.1, ECO:0000313|Proteomes:UP000000724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC {ECO:0000313|Proteomes:UP000000724};
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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; AM920431; CAP93284.1; -; Genomic_DNA.
DR RefSeq; XP_002560950.1; XM_002560904.1.
DR AlphaFoldDB; B6H8T0; -.
DR STRING; 500485.B6H8T0; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GeneID; 8314415; -.
DR KEGG; pcs:Pc16g06140; -.
DR VEuPathDB; FungiDB:PCH_Pc16g06140; -.
DR eggNOG; KOG0471; Eukaryota.
DR HOGENOM; CLU_006462_7_2_1; -.
DR OMA; NAQLCQT; -.
DR OrthoDB; 3249969at2759; -.
DR BioCyc; PCHR:PC16G06140-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c16.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF220; ALPHA-AMYLASE; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..547
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002843494"
FT TRANSMEM 525..546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..395
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 233
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT ACT_SITE 257
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT SITE 323
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-2"
FT DISULFID 54..62
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 178..191
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 465..500
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
SQ SEQUENCE 547 AA; 60690 MW; 79FB7B9D19EDF351 CRC64;
MSRSTVGPLV GLLLIACLIS SASAARTADW KPRSIYQTMT DRFARTDGST TSPCNTKAGL
YCGGTWRGTI DRLDYIQGMG FDAVMISPII ENVEGQVEYG EAYHGYWPLN LNNLNSHFGT
HQDLLDLSDA LHSRGMYFMM DTVINNMAYI TNGSDPATDV DYSVFTPFNN ADYFHPYCTM
NWSVPAIAQK CNTGDDKVVL PDLFTEHEDV QQLLIKWAND AIKTYSIDGL RIDAAKHVNP
DFLRKFSDGV DTFMTGEVLE GAVSIMEDYQ SNYINSLPNY PVYFQILAAF TNGTTPPLAK
AVEDMRVAVP DVNAMASFSE NHDKARIASY NDDMSIAKNV LVFTMLFDGI PMIYQGQEQH
LKGDGVPHNR EAIWLTKYDT EAELYKLIAK LNRIRSHAGY LGSDYFEDAT HPIYQGSSEL
AFTKGVQGRQ VVMVLSNQPS TSGRYDLDLT VSYNAGTEVM DVLNCNNYTV DNQGMLRVDM
DKGEPRVFFP TKYMEGSGLC GYSDANITLE MLKTHRTSMS AGTQLTSGTG VATFLLAVVT
SIFVTFL
//
