AMYP_STRCA
ID AMYP_STRCA Reviewed; 497 AA.
AC P83053;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Pancreatic alpha-amylase;
DE Short=PA;
DE EC=3.2.1.1 {ECO:0000269|Ref.2};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
OS Struthio camelus (Common ostrich).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=8801 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC TISSUE=Pancreas;
RX PubMed=11281265; DOI=10.1016/s0305-0491(00)00282-0;
RA Kabuto S., Ogawa T., Muramoto K., Oosthuizen V., Naude R.J.;
RT "The amino acid sequence of pancreatic alpha-amylase from the ostrich,
RT Struthio camelus.";
RL Comp. Biochem. Physiol. 127B:481-490(2000).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-53, AND CATALYTIC ACTIVITY.
RC TISSUE=Pancreas;
RA Oosthuizen V., Naude R.J., Oelofsen W., Muramoto K., Kamiya H.;
RT "Ostrich pancreatic alpha-amylase: kinetic properties, amino terminal
RT sequence and subsite structure.";
RL Int. J. Biochem. 26:1313-1321(1994).
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|Ref.2};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P04746};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P04746};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000250|UniProtKB:P04746};
CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P04746};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR AlphaFoldDB; P83053; -.
DR SMR; P83053; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; P83053; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1180; -; 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 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; SSF51445; 1.
PE 1: Evidence at protein level;
KW Calcium; Carbohydrate metabolism; Chloride; Direct protein sequencing;
KW Disulfide bond; Glycosidase; Hydrolase; Metal-binding;
KW Pyrrolidone carboxylic acid; Secreted.
FT CHAIN 1..497
FT /note="Pancreatic alpha-amylase"
FT /id="PRO_0000054291"
FT ACT_SITE 197
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT ACT_SITE 233
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 195
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 298
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT BINDING 337
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT SITE 300
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:11281265"
FT DISULFID 28..86
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 70..115
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 141..160
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 379..385
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 451..463
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT CONFLICT 35
FT /note="Y -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 50..52
FT /note="IIT -> VFN (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 55898 MW; 62DB18FCD80BCA8B CRC64;
QYNPNTQPGR TSIVHLFEWR WADIALECER YLAPYGFGGV QVSPPNENVI ITNPYRPWWE
RYQPVSYKLC TRSGNENEFR DMVTRCNNVG VRIYVDAVKN HMCGSGAGSG THSTCGAYFN
AGNRDSPAVP YSGWDFNDGK CRTGSGEIEN YGDASQVRDC RLVGLLDLAL EKDYVRSTVA
GYMNHLIDIG VAGFRLDAAK HMWPGDIKAF LDKLHNLNTN WFSSGSRPFI YQEVIDLGGE
PITSSQYFGN HRVTEFKYGA KLGTVIRKWN GEKMAYLKNW GEGWGFVPSD RALVFVDNHD
NQRGHGAGGA SILTFWDARL YKMAVGFMLA HPYGFTRVMS SFRWPRHFEN GKDVNDWYGP
PSNSDGSTKE VTINADSTCG NDWVCEHRWR QIRNMVIFRN VVDGEPFSNW WDNNSNQVAF
GRGSKGFIVF NNDDWHMNVD LYTGLPAGTY CDVISGQKEG SRCTGIQVYV SGNGKANFQI
SNNAEDPFIA IHVGAKL
