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P23671 (AMY_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 onPlasmid pSOL1
OrganismClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) [Reference proteome] [HAMAP]
Taxonomic identifier272562 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length760 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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 processCarbohydrate metabolism
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Plasmid
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionalpha-amylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

starch binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Potential
Chain35 – 760726Alpha-amylase
PRO_0000001338

Sites

Active site2221Nucleophile By similarity
Active site2621Proton donor By similarity
Metal binding1431Calcium By similarity
Metal binding1841Calcium; via carbonyl oxygen By similarity
Metal binding1921Calcium By similarity
Metal binding2261Calcium; via carbonyl oxygen By similarity
Site3211Transition state stabilizer By similarity

Experimental info

Sequence conflict2131D → H in AAA63759. Ref.1
Sequence conflict2221D → H in AAA63759. Ref.1
Sequence conflict5711A → G in AAA63759. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P23671 [UniParc].

Last modified August 29, 2001. Version 2.
Checksum: 10E146F40252F6D0

FASTA76083,045
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 292-760.
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

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.
PIRB37837.
RefSeqNP_149331.1. NC_001988.2.

3D structure databases

ProteinModelPortalP23671.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272562.CA_P0168.

Protein family/group databases

CAZyCBM25. Carbohydrate-Binding Module Family 25.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK76913; AAK76913; CA_P0168.
GeneID1116173.
KEGGcac:CA_P0168.
PATRIC32034222. VBICloAce74127_0169.

Phylogenomic databases

eggNOGCOG0366.
HOGENOMHOG000292529.
KOK01176.
OMAGQNIFVV.
OrthoDBEOG6F55CH.

Enzyme and pathway databases

BioCycCACE272562:GJIH-4013-MONOMER.

Family and domain databases

Gene3D2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProIPR006048. A-amylase_b_C.
IPR006046. Alpha_amylase.
IPR005085. CBM_fam25.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00128. Alpha-amylase. 1 hit.
PF03423. CBM_25. 3 hits.
[Graphical view]
PRINTSPR00110. ALPHAAMYLASE.
SMARTSM00632. Aamy_C. 1 hit.
SM01066. CBM_25. 3 hits.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMY_CLOAB
AccessionPrimary (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: May 14, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries