P30269 (AMY_BUTFI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-amylase
EC=3.2.1.1

Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase

Gene names

Name:

amyA

Organism

Butyrivibrio fibrisolvens

Taxonomic identifier

831 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Lachnospiraceae › Butyrivibrio

Protein attributes

Sequence length	976 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Glycosidase Hydrolase
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 metal 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
	Signal peptide	1 – 33	33	Potential
	Chain	34 – 976	943	Alpha-amylase		PRO_0000001337
Sites
	Active site	323	1	Nucleophile By similarity
	Active site	375	1	Proton donor By similarity
	Metal binding	243	1	Calcium By similarity
	Metal binding	284	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	293	1	Calcium By similarity
	Metal binding	327	1	Calcium; via carbonyl oxygen By similarity
	Site	447	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	P30269 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 61D690FDC19315AC	FASTA	976	106,695
	10 20 30 40 50 60 MKRGKLWGRL VSAAGLSLSI FLSSIGNVST AYAMESNDAL VLDETKENTE SATDASSNEA 70 80 90 100 110 120 SDAEADNDTD EAITDASSKE LSAENDGASE SDSSFDEYDH TALPETDEIT VTAAGELSTA 130 140 150 160 170 180 KAELYTLAPR EAREADNSLV TRDSIHDGAI LHAFCWSFNT IADNMADIAD AGYTAVQTSP 190 200 210 220 230 240 INECLSTNPG MNLHGPDGMW YYHYQPTDWV IGNYQLGSRD EFKHMCDVAD EYGVAVIVDI 250 260 270 280 290 300 LPNHTTPSTG SIAKALMEAA GGSDALYHAT GKIGGGYTDR LELTYYSMGG LPDVDTENTG 310 320 330 340 350 360 FQQYFYEFLK DCVYLGADGF RIDTAKHISL PDDPVPSDYS DAGRNTFYPN MREALNEYSE 370 380 390 400 410 420 EVGTKSYDEL FVYGEVLQGT NDRLAAYQQY IGGTTASNYG SSLRSALSSG NLSVNRLLDY 430 440 450 460 470 480 QIYDDTAYGS TYTADTEKLV TWVESHDNYM NDSESCWKSI DDDMVIMGWS IIAARDAGTP 490 500 510 520 530 540 LFFSRPNNSS AENPYGDNLI GAAGSPIYKA PEVKAVNLFR EKMGEADEYL SNPGGNIQTL 550 560 570 580 590 600 MIERYNDTVQ GAVIVNAAQT RTTISTETHL SDGIYPDQVE GSNSVFLVKD GVLSGSVEGE 610 620 630 640 650 660 GVVVLSEKMD GTGKVVSFYN NKNWNGVVAR VDNAEETLDT IDENDGWFQV TVLDDEFTIR 670 680 690 700 710 720 FESADGKEVS PEFQITAESG TFATPDSSEL YYSKAEAEEG LGIHTYPVYF FNTENWGSVY 730 740 750 760 770 780 TYGWLDGGAQ LFGGWPGTVA VNEGSGWYRA DVKTTGEITA FNLIFNNGNG IQTVNVEGIT 790 800 810 820 830 840 PDSKDIYLAV DAEKSNGQLI VNRYEDKESA EKALGVSGSY TTAYFYNTEG WDKVCAYTWG 850 860 870 880 890 900 ATALGDWPGK ELTQDEDGWY SVVLPAGPSE DLNIIFNNGN NGKQTNDMKI SDMKYRFILN 910 920 930 940 950 960 NGISYQKYGS KKDAMEAIAG AGDVTYETVY FYNEKADDAN WKNVYLYVFG GTDGEYNNLV 970 GTWPGKLMEK EEDSNG

References

[1]	"Cloning, nucleotide sequence, and enzymatic characterization of an alpha-amylase from the ruminal bacterium Butyrivibrio fibrisolvens H17c." Rumbak E., Rawlings D.E., Lindsey G.G., Woods D.R. J. Bacteriol. 173:4203-4211(1991) [PubMed: 2061294] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: H17C.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M62507 Genomic DNA. Translation: AAA23005.1.
PIR	A42466.
3D structure databases
ProteinModelPortal	P30269.
ModBase	Search...
Protein family/group databases
CAZy	CBM26. Carbohydrate-Binding Module Family 26. GH13. Glycoside Hydrolase Family 13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR015902. Alpha_amylase. IPR006046. Glyco_hydro_13. IPR013780. Glyco_hydro_13_b. IPR006047. Glyco_hydro_13_cat_dom. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHER	PTHR10357. Alpha_amylase. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. [Graphical view]
PRINTS	PR00110. ALPHAAMYLASE.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AMY_BUTFI

Accession

Primary (citable) accession number: P30269

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	December 14, 2011
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program