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 02-SEP-2026, entry version 107. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; P83053; -. DR SMR; P83053; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1. DR FunFam; 2.60.40.1180:FF:000020; Pancreatic alpha-amylase; 1. DR FunFam; 3.20.20.80:FF:000056; Pancreatic alpha-amylase; 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; GH13_cat_dom. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR013780; Glyco_hydro_b. DR PANTHER; PTHR43447; 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 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 //