Carbonic anhydrase 2 - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P61517 (CAN_ECOLI)

Last modified November 3, 2009. Version 59. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.

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Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	carbon utilization Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	carbonate dehydratase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
tufA	P0A6N1	1	EBI-562106,EBI-301077

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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...

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Sequences

Sequence

Length

Mass (Da)

Tools

P61517-1 [UniParc].

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

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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: 8202364] [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: 9278503] [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: 16738553] [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: 10493123] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[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: 11316870] [Abstract] Cited for: FUNCTION, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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

PIR

F64735.

RefSeq

AP_000787.1.
NP_414668.1.

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P61517. 10 interactions.

STRING

P61517.

Genome annotation databases

GeneID

944832.

GenomeReviews

Gene locus JW0122 in contig AP009048_GR.
Gene locus b0126 in contig U00096_GR.

KEGG

ecj:JW0122.
eco:b0126.

Organism-specific databases

EchoBASE

EB2224.

EcoGene

EG12319. can.

CMR

Search...

Phylogenomic databases

HOGENOM

P61517.

OMA

VQEAWAR.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12319-MON.

BRENDA

4.2.1.1. 246.

Gene expression databases

Genevestigator

P61517.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.40.1050.10. CO_anhd_prok_pln. 1 hit.

PANTHER

PTHR11002. Carbonic_anhydrase. 1 hit.

Pfam

PF00484. Pro_CA. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

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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:	November 3, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

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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 and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents