Carbonic anhydrase 2 - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P61517 (CAN_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Carbonic anhydrase 2
EC=4.2.1.1

Alternative name(s):
Carbonate dehydratase 2

Gene names

Name:	can
Synonyms:	cynT2, yadF
Ordered Locus Names:	b0126, JW0122

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	H₂CO₃ = CO₂ + H₂O.
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the beta-class carbonic anhydrase family.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbon utilization Inferred from electronic annotation. Source: InterPro
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	carbonate dehydratase activity Inferred from direct assay Ref.5. Source: EcoCyc zinc ion binding Inferred from direct assay Ref.5 PubMed 22094925. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 220

220

Carbonic anhydrase 2

PRO_0000077465

Sites

Metal binding

Zinc

Metal binding

Zinc

Metal binding

Zinc

Metal binding

101

Zinc

Secondary structure

220

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P61517 [UniParc].

Last modified May 24, 2004. Version 1.
Checksum: 48A9086BE9428452
Show »

FASTA

220

25,097

        10         20         30         40         50         60 
MKDIDTLISN NALWSKMLVE EDPGFFEKLA QAQKPRFLWI GCSDSRVPAE RLTGLEPGEL 

        70         80         90        100        110        120 
FVHRNVANLV IHTDLNCLSV VQYAVDVLEV EHIIICGHYG CGGVQAAVEN PELGLINNWL 

       130        140        150        160        170        180 
LHIRDIWFKH SSLLGEMPQE RRLDTLCELN VMEQVYNLGH STIMQSAWKR GQKVTIHGWA 

       190        200        210        220 
YGIHDGLLRD LDVTATNRET LEQRYRHGIS NLKLKHANHK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Fujita N., Mori H., Yura T., Ishihama A. Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography." Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B. Electrophoresis 20:2181-2195(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Strain: B / BL21.
[5]	"Crystal structure of E. coli beta-carbonic anhydrase, an enzyme with an unusual pH-dependent activity." Cronk J.D., Endrizzi J.A., Cronk M.R., O'neill J.W., Zhang K.Y.J. Protein Sci. 10:911-922(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00096 Genomic DNA. Translation: AAC73237.1.
AP009048 Genomic DNA. Translation: BAB96701.2.

PIR

F64735.

RefSeq

NP_414668.1. NC_000913.2.
YP_488429.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I6O	X-ray	2.20	A/B	1-220	[»]
1I6P	X-ray	2.00	A	1-220	[»]
1T75	X-ray	2.50	A/B/D/E	1-220	[»]
2ESF	X-ray	2.25	A/B	1-220	[»]

ProteinModelPortal

P61517.

SMR

P61517. Positions 2-215.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36168N.

IntAct

P61517. 10 interactions.

STRING

511145.b0126.

Proteomic databases

PaxDb

P61517.

PRIDE

P61517.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73237; AAC73237; b0126.
BAB96701; BAB96701; BAB96701.

GeneID

12930739.
944832.

KEGG

ecj:Y75_p0123.
eco:b0126.

PATRIC

32115355. VBIEscCol129921_0129.

Organism-specific databases

EchoBASE

EB2224.

EcoGene

EG12319. can.

Phylogenomic databases

eggNOG

COG0288.

HOGENOM

HOG000125184.

K01673.

OMA

VQEAWAR.

ProtClustDB

PRK10437.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12319-MONOMER.
ECOL316407:JW0122-MONOMER.

BRENDA

4.2.1.1. 2026.

Gene expression databases

Genevestigator

P61517.

Family and domain databases

Gene3D

3.40.1050.10. 1 hit.

InterPro

IPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]

PANTHER

PTHR11002. PTHR11002. 1 hit.

Pfam

PF00484. Pro_CA. 1 hit.
[Graphical view]

SMART

SM00947. Pro_CA. 1 hit.
[Graphical view]

SUPFAM

SSF53056. Prok_plnt_COanhd. 1 hit.

PROSITE

PS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P61517.

Entry information

Entry name

CAN_ECOLI

Accession

Primary (citable) accession number: P61517
Secondary accession number(s): P36857, P75656, Q8KJQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	May 24, 2004
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents