Reviewed, UniProtKB/Swiss-Prot P83053 (AMYP_STRCA)

Names and origin

Protein names	Recommended name:     Pancreatic alpha-amylase       Short name=PA     EC=3.2.1.1 Alternative name(s):     1,4-alpha-D-glucan glucanohydrolase
Organism	Struthio camelus (Ostrich)
Taxonomic identifier	8801 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Palaeognathae › Struthioniformes › Struthionidae › Struthio

Protein attributes

Sequence length	497 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.
Cofactor	Binds 1 calcium ion per subunit By similarity. Binds 1 chloride ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Secreted › extracellular space.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Secreted
Ligand	Calcium Chloride Metal-binding
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Pyrrolidone carboxylic acid
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW chloride ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 497	497	Pancreatic alpha-amylase		PRO_0000054291
Sites
	Active site	197	1	Nucleophile By similarity UniProtKB P00690
	Active site	233	1	Proton donor By similarity
	Active site	300	1	By similarity UniProtKB P00690
	Metal binding	100	1	Calcium By similarity
	Metal binding	158	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	167	1	Calcium By similarity
	Metal binding	201	1	Calcium; via carbonyl oxygen By similarity
	Binding site	195	1	Chloride By similarity
	Binding site	298	1	Chloride By similarity
	Binding site	337	1	Chloride By similarity
Amino acid modifications
	Modified residue	1	1	Pyrrolidone carboxylic acid Ref.1
	Disulfide bond	28 ↔ 86		By similarity UniProtKB P00690
	Disulfide bond	70 ↔ 115		By similarity UniProtKB P00690
	Disulfide bond	141 ↔ 160		By similarity UniProtKB P00690
	Disulfide bond	379 ↔ 385		By similarity UniProtKB P00690
	Disulfide bond	451 ↔ 463		By similarity UniProtKB P00690
Experimental info
	Sequence conflict	35	1	Y → K AA sequence Ref.2
	Sequence conflict	50 – 52	3	IIT → VFN AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P83053-1 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 62DB18FCD80BCA8B	FASTA	497	55,898
	10 20 30 40 50 60 QYNPNTQPGR TSIVHLFEWR WADIALECER YLAPYGFGGV QVSPPNENVI ITNPYRPWWE 70 80 90 100 110 120 RYQPVSYKLC TRSGNENEFR DMVTRCNNVG VRIYVDAVKN HMCGSGAGSG THSTCGAYFN 130 140 150 160 170 180 AGNRDSPAVP YSGWDFNDGK CRTGSGEIEN YGDASQVRDC RLVGLLDLAL EKDYVRSTVA 190 200 210 220 230 240 GYMNHLIDIG VAGFRLDAAK HMWPGDIKAF LDKLHNLNTN WFSSGSRPFI YQEVIDLGGE 250 260 270 280 290 300 PITSSQYFGN HRVTEFKYGA KLGTVIRKWN GEKMAYLKNW GEGWGFVPSD RALVFVDNHD 310 320 330 340 350 360 NQRGHGAGGA SILTFWDARL YKMAVGFMLA HPYGFTRVMS SFRWPRHFEN GKDVNDWYGP 370 380 390 400 410 420 PSNSDGSTKE VTINADSTCG NDWVCEHRWR QIRNMVIFRN VVDGEPFSNW WDNNSNQVAF 430 440 450 460 470 480 GRGSKGFIVF NNDDWHMNVD LYTGLPAGTY CDVISGQKEG SRCTGIQVYV SGNGKANFQI 490 SNNAEDPFIA IHVGAKL

References

[1]	"The amino acid sequence of pancreatic alpha-amylase from the ostrich, Struthio camelus." Kabuto S., Ogawa T., Muramoto K., Oosthuizen V., Naude R.J. Comp. Biochem. Physiol. 127B:481-490(2000) [PubMed: 11281265] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Pancreas.
[2]	"Ostrich pancreatic alpha-amylase: kinetic properties, amino terminal sequence and subsite structure." Oosthuizen V., Naude R.J., Oelofsen W., Muramoto K., Kamiya H. Int. J. Biochem. 26:1313-1321(1994) Cited for: PROTEIN SEQUENCE OF 1-53. Tissue: Pancreas.

Cross-references

3D structure databases
HSSP	HSSP built from PDB template 1HNY based on UniProtKB P04746.
SMR	P83053. Positions 1-497.
ModBase	Search...
Phylogenomic databases
HOVERGEN	P83053.
Enzyme and pathway databases
BRENDA	3.2.1.1. 39275.
Family and domain databases
InterPro	IPR006048. A-amylase_b_C. IPR006046. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat. IPR006589. Glyco_hydro_13_sub_cat. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF02806. Alpha-amylase_C. 1 hit. [Graphical view]
PRINTS	PR00110. ALPHAAMYLASE.
SMART	SM00642. Aamy. 1 hit. SM00632. Aamy_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMYP_STRCA

Accession

Primary (citable) accession number: P83053

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 17, 2003
Last sequence update:	October 1, 2001
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)