AMYA_ASPNG
ID AMYA_ASPNG Reviewed; 484 AA.
AC P56271;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Acid alpha-amylase;
DE EC=3.2.1.1 {ECO:0000269|PubMed:2207069};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS,
RP CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
RX PubMed=2207069; DOI=10.1021/bi00478a019;
RA Boel E., Brady L., Brzozowski A.M., Derewenda Z., Dodson G.G., Jensen V.J.,
RA Petersen S.B., Swift H., Thim L., Woldike H.F.;
RT "Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A
RT resolution of two enzymes from Aspergillus.";
RL Biochemistry 29:6244-6249(1990).
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:0000269|PubMed:2207069};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:2207069};
CC Note=Binds 2 calcium ions per subunit. Calcium is inhibitory at high
CC concentrations. {ECO:0000269|PubMed:2207069};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:2207069}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2207069}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR PIR; A35282; A35282.
DR PDB; 2AAA; X-ray; 2.10 A; A=1-484.
DR PDBsum; 2AAA; -.
DR AlphaFoldDB; P56271; -.
DR SMR; P56271; -.
DR STRING; 5061.CADANGAP00008517; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR VEuPathDB; FungiDB:An11g03340; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1147022; -.
DR VEuPathDB; FungiDB:ATCC64974_89550; -.
DR VEuPathDB; FungiDB:M747DRAFT_340768; -.
DR eggNOG; KOG0471; Eukaryota.
DR EvolutionaryTrace; P56271; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 Gene3D; 2.60.40.1180; -; 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 Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF09260; DUF1966; 1.
DR PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Metal-binding; Secreted.
FT CHAIN 1..484
FT /note="Acid alpha-amylase"
FT /id="PRO_0000054289"
FT ACT_SITE 206
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:2207069"
FT ACT_SITE 230
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:2207069"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:2207069,
FT ECO:0007744|PDB:2AAA"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:2207069,
FT ECO:0007744|PDB:2AAA"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:2207069,
FT ECO:0007744|PDB:2AAA"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 206
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:2207069,
FT ECO:0007744|PDB:2AAA"
FT BINDING 209..210
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:2207069,
FT ECO:0007744|PDB:2AAA"
FT BINDING 230
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:2207069,
FT ECO:0007744|PDB:2AAA"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT SITE 297
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P0C1B3"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..38
FT /evidence="ECO:0000269|PubMed:2207069,
FT ECO:0007744|PDB:2AAA"
FT DISULFID 150..164
FT /evidence="ECO:0000269|PubMed:2207069,
FT ECO:0007744|PDB:2AAA"
FT DISULFID 240..283
FT /evidence="ECO:0000269|PubMed:2207069,
FT ECO:0007744|PDB:2AAA"
FT DISULFID 440..475
FT /evidence="ECO:0000269|PubMed:2207069,
FT ECO:0007744|PDB:2AAA"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:2AAA"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:2AAA"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:2AAA"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 158..163
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 181..198
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 252..262
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 269..282
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 308..320
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:2AAA"
FT TURN 329..334
FT /evidence="ECO:0007829|PDB:2AAA"
FT TURN 339..343
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 357..375
FT /evidence="ECO:0007829|PDB:2AAA"
FT TURN 377..381
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 393..400
FT /evidence="ECO:0007829|PDB:2AAA"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:2AAA"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:2AAA"
FT STRAND 461..465
FT /evidence="ECO:0007829|PDB:2AAA"
FT HELIX 466..469
FT /evidence="ECO:0007829|PDB:2AAA"
SQ SEQUENCE 484 AA; 52935 MW; 04D596E34680656D CRC64;
LSAASWRTQS IYFLLTDRFG RTDNSTTATC NTGNEIYCGG SWQGIIDHLD YIEGMGFTAI
WISPITEQLP QDTADGEAYH GYWQQKIYDV NSNFGTADNL KSLSDALHAR GMYLMVDVVP
DHMGYAGNGN DVDYSVFDPF DSSSYFHPYC LITDWDNLTM VEDCWEGDTI VSLPDLDTTE
TAVRTIWYDW VADLVSNYSV DGLRIDSVLE VQPDFFPGYN KASGVYCVGE IDNGNPASDC
PYQKVLDGVL NYPIYWQLLY AFESSSGSIS NLYNMIKSVA SDCSDPTLLG NFIENHDNPR
FAKYTSDYSQ AKNVLSYIFL SDGIPIVYAG EEQHYAGGKV PYNREATWLS GYDTSAELYT
WIATTNAIRK LAIAADSAYI TYANDAFYTD SNTIAMAKGT SGSQVITVLS NKGSSGSSYT
LTLSGSGYTS GTKLIEAYTC TSVTVDSSGD IPVPMASGLP RVLLPASVVD SSSLCGGSGR
LYVE
