P23671 (AMY_CLOAB) 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
Synonyms:	amyP
Ordered Locus Names:	CA_P0168

Encoded on

Plasmid pSOL1

Organism

Clostridium acetobutylicum

Taxonomic identifier

1488 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	760 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
Technical term	Complete proteome Plasmid Reference proteome
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 – 34	34	Potential
	Chain	35 – 760	726	Alpha-amylase		PRO_0000001338
Sites
	Active site	222	1	Nucleophile By similarity
	Active site	262	1	Proton donor By similarity
	Metal binding	143	1	Calcium By similarity
	Metal binding	184	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	192	1	Calcium By similarity
	Metal binding	226	1	Calcium; via carbonyl oxygen By similarity
	Site	321	1	Transition state stabilizer By similarity
Experimental info
	Sequence conflict	213	1	D → H in AAA63759. Ref.1
	Sequence conflict	222	1	D → H in AAA63759. Ref.1
	Sequence conflict	571	1	A → G in AAA63759. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P23671 [UniParc]. Last modified August 29, 2001. Version 2. Checksum: 10E146F40252F6D0	FASTA	760	83,045
	10 20 30 40 50 60 MSKRSKLLKR RMLSLSVICV LIGYGPVFNP VRSQAKVMTY SSENRELPEN TKDGVMLHAF 70 80 90 100 110 120 DWSFNNIKKE LPSIAAAGYK AVQVSPVQGT KSNSTNSSDW WLLYQPTNQA IGNAQLGSYD 130 140 150 160 170 180 DFKSLCSEAK NYGISIVVDV VMNHMANNGN DDEVASEVDP SFKDPSLYHH NGQCTDWNNR 190 200 210 220 230 240 QDVTQEGIGM PDLNTQSSAV QSKAITFLNQ CVDAGATGFR FDAAKHIETD LGLDANKSWS 250 260 270 280 290 300 GNYWENVLGS LHNKSNLYIY GEVLQDGKVD NISAYESFMN VEASAYDGSL RGAIKSGDLT 310 320 330 340 350 360 NAQGMGGLDS NKCVDMLETH DEYEHNESKD LTDWQRKAGW AIAASRAGSV PLFFDRPTGN 370 380 390 400 410 420 IGSEGDALWK DSDVVAVNEF HNAMAGQNEY LRLQNNNKAM IIERGSKGAV IVNEGDSFNL 430 440 450 460 470 480 NTPTNLEDGN YDNHGSATDS LTVSQGRMTG TVPANSIIVI YNKNSNPGSD RVTLSEQAAK 490 500 510 520 530 540 AGDSVTITYD AGTTALKDAS NVNLYWGYDG FSAATSKAMT SLGDNKWQTT ITVPKEVTKN 550 560 570 580 590 600 VNFSFTDGTS WDNNNGANWN IPLASNYLPH AGYKVDYDSS NLVSGNNFTI YYNGNLANSS 610 620 630 640 650 660 NVSLHWGVNG WSNMQNLAMV KDSNGFWEAT IAIPASSNTL NFCFTNGSSW DNNNNNNWTL 670 680 690 700 710 720 NTWSSVPKVQ VTPAPEACKQ ISVYYNGSLA SSASNITLHW GCNGFTSPQD INMVKQADGR 730 740 750 760 WLANITLPSG CYNVNMAFKD QSGTWDNNNS NNYNFSSTNN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence analysis and ECF sigma factor-dependent expression of an alpha-amylase gene from Clostridium acetobutylicum DSM 792." Schaffer S., Duerre P. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
[2]	"Molecular characterization of amyP, a pSOL1 located gene coding the major alpha-amylase of Clostridium acetobutylicum ATCC824, and its use as a reporter system for strain degeneration." Sabathe F., Cornillot E., Croux C., Soucaille P. Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
[3]	"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum." Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R. J. Bacteriol. 183:4823-4838(2001) [PubMed: 11466286] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
[4]	"Cloning, sequencing, and molecular analysis of the acetoacetate decarboxylase gene region from Clostridium acetobutylicum." Gerischer U., Duerre P. J. Bacteriol. 172:6907-6918(1990) [PubMed: 2254264] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 292-760. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M55392 Genomic DNA. Translation: AAA63759.2. AF164199 Genomic DNA. Translation: AAD47072.1. AE001438 Genomic DNA. Translation: AAK76913.1.
PIR	B37837.
RefSeq	NP_149331.1. NC_001988.2.
3D structure databases
ProteinModelPortal	P23671.
ModBase	Search...
Protein family/group databases
CAZy	CBM25. Carbohydrate-Binding Module Family 25. GH13. Glycoside Hydrolase Family 13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1116173.
GenomeReviews	Gene locus CA_P0168 in contig AE001438_GR.
KEGG	cac:CA_P0168.
NMPDR	fig|272562.1.peg.166.
PATRIC	32034222. VBICloAce74127_0169.
Phylogenomic databases
HOGENOM	HBG417661.
OMA	HMANNGN.
ProtClustDB	CLSK2517243.
Enzyme and pathway databases
BioCyc	CACE272562:CAP0168-MONOMER.
Family and domain databases
InterPro	IPR006048. A-amylase_b_C. IPR015902. Alpha_amylase. IPR005085. CBM_fam25. 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.
KO	K01176.
PANTHER	PTHR10357. Alpha_amylase. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF03423. CBM_25. 3 hits. [Graphical view]
PRINTS	PR00110. ALPHAAMYLASE.
SMART	SM00632. Aamy_C. 1 hit. SM01066. CBM_25. 3 hits. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AMY_CLOAB

Accession

Primary (citable) accession number: P23671
Secondary accession number(s): Q9S429

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	August 29, 2001
Last modified:	January 25, 2012
This is version 91 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program