Reviewed, UniProtKB/Swiss-Prot P49067 (AMYA_PYRFU)

Names and origin

Protein names

Recommended name:
    Alpha-amylase
    EC=3.2.1.1

Gene names

Name:	amyA
Ordered Locus Names:	PF0272

Organism

Pyrococcus furiosus [Complete proteome] [HAMAP]

Taxonomic identifier

2261 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	649 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Displays a broad range of substrate specificity, with the capacity to hydrolyze carbohydrates as simple as maltotriose.
Catalytic activity	Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in oligosaccharides and polysaccharides.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the glycosyl hydrolase 57 family.
Biophysicochemical properties	pH dependence: Optimum pH is 6.5-7.5. Temperature dependence: Optimum temperature is 100 degrees Celsius. Inactive below 40 degrees Celsius. Extremely thermostable.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC carbohydrate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 649	648	Alpha-amylase		PRO_0000184573
Sites
	Active site	124	1	Nucleophile By similarity
	Active site	215	1	Proton donor By similarity

Sequences

	Sequence		Length	Mass (Da)
	P49067-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: B75840D33D17146F	FASTA	649	76,309
	10 20 30 40 50 60 MGDKINFIFG IHNHQPLGNF GWVFEEAYEK CYWPFLETLE EYPNMKVAIH TSGPLIEWLQ 70 80 90 100 110 120 DNRPEYIDLL RSLVKRGQVE IVVAGFYEPV LASIPKEDRI EQIRLMKEWA KSIGFDARGV 130 140 150 160 170 180 WLTERVWQPE LVKTLKESGI DYVIVDDYHF MSAGLSKEEL YWPYYTEDGG EVIAVFPIDE 190 200 210 220 230 240 KLRYLIPFRP VDKVLEYLHS LIDGDESKVA VFHDDGEKFG IWPGTYEWVY EKGWLREFFD 250 260 270 280 290 300 RISSDEKINL MLYTEYLEKY KPRGLVYLPI ASYFEMSEWS LPAKQARLFV EFVNELKVKG 310 320 330 340 350 360 IFEKYRVFVR GGIWKNFFYK YPESNYMHKR MLMVSKLVRN NPEARKYLLR AQCNDAYWHG 370 380 390 400 410 420 LFGGVYLPHL RRAIWNNLIK ANSYVSLGKV IRDIDYDGFE EVLIENDNFY AVFKPSYGGS 430 440 450 460 470 480 LVEFSSKNRL VNYVDVLARR WEHYHGYVES QFDGVASIHE LEKKIPDEIR KEVAYDKYRR 490 500 510 520 530 540 FMLQDHVVPL GTTLEDFMFS RQQEIGEFPR VPYSYELLDG GIRLKREHLG IEVEKTVKLV 550 560 570 580 590 600 NDGFEVEYIV NNKTGNPVLF AVELNVAVQS IMESPGVLRG KEIVVDDKYA VGKFALKFED 610 620 630 640 EMEVWKYPVK TLSQSESGWD LIQQGVSYIV PIRLEDKIRF KLKFEEASG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus. Cloning and sequencing of the gene and expression in Escherichia coli." Laderman K.A., Asada K., Uemori T., Mukai H., Taguchi Y., Kato I., Anfinsen C.B. J. Biol. Chem. 268:24402-24407(1993) [PubMed: 8226990] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]	"The complete sequence of the Pyrococcus furiosus genome." Weiss R.B., Dunn D.M., Robb F.T., Brown J.R. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[3]	"The purification and characterization of an extremely thermostable alpha-amylase from the hyperthermophilic archaebacterium Pyrococcus furiosus." Laderman K.A., Davis B.R., Krutzsch H.C., Lewis M.S., Griko Y.V., Privalov P.L., Anfinsen C.B. J. Biol. Chem. 268:24394-24401(1993) [PubMed: 8226989] [Abstract] Cited for: CHARACTERIZATION. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L22346 Unassigned DNA. Translation: AAA72035.1. AE009950 Genomic DNA. Translation: AAL80396.1. Different initiation.
PIR	A49512.
RefSeq	NP_578001.1.
3D structure databases
SMR	P49067. Positions 3-646.
ModBase	Search...
Protein family/group databases
CAZy	GH57. Glycoside Hydrolase Family 57.
Genome annotation databases
GeneID	1468106.
GenomeReviews	Gene locus PF0272 in contig AE009950_GR.
KEGG	pfu:PF0272.
NMPDR	fig|186497.1.peg.277.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG460637.
OMA	LRYLIPF.
Enzyme and pathway databases
BRENDA	3.2.1.1. 321.
Family and domain databases
InterPro	IPR015179. A-amylase/a-glucanoTrfase_prok. IPR015178. DUF1925. IPR011013. Glyco_hydro-type_carb-bd. IPR011330. Glyco_hydro/deAcase_b/a-brl. IPR004300. Glyco_hydro_57_core. [Graphical view]
Pfam	PF09094. DUF1925. 1 hit. PF09095. DUF1926. 1 hit. PF03065. Glyco_hydro_57. 1 hit. [Graphical view]
ProDom	PD014405. DUF1925. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...

Entry information

Entry name

AMYA_PYRFU

Accession

Primary (citable) accession number: P49067

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)