Reviewed, UniProtKB/Swiss-Prot P0ABE9 (CYNT_ECOLI)

Names and origin

Protein names

Recommended name:
    Carbonic anhydrase 1
    EC=4.2.1.1
Alternative name(s):
    Carbonate dehydratase 1

Gene names

Name:	cynT
Ordered Locus Names:	b0339, JW0330

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	219 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Reversible hydration of carbon dioxide. Carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (cynS) diffuses out of the cell faster than it would be hydrated to bicarbonate, so the apparent function of this enzyme is to catalyze the hydration of carbon dioxide and thus prevent depletion of cellular bicarbonate.
Catalytic activity	H2CO3 = CO2 + H2O.
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Oligomer.
Induction	By cyanate.
Sequence similarities	Belongs to the beta-class carbonic anhydrase family.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carbon utilization Inferred from electronic annotation. Source: InterPro
Molecular function	carbonate dehydratase activity Inferred from electronic annotation. Source: EC zinc 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
	Chain	1 – 219	219	Carbonic anhydrase 1		PRO_0000077459
Sites
	Metal binding	39	1	Zinc By similarity
	Metal binding	41	1	Zinc By similarity
	Metal binding	98	1	Zinc By similarity
	Metal binding	101	1	Zinc By similarity
Experimental info
	Sequence conflict	174 – 176	3	RIA → GS in AAA23625. Ref.1
	Sequence conflict	212	1	P → R in AAA23625. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P0ABE9-1 [UniParc]. Last modified October 25, 2005. Version 1. Checksum: 5EB41F125EC4D731	FASTA	219	23,764
	10 20 30 40 50 60 MKEIIDGFLK FQREAFPKRE ALFKQLATQQ SPRTLFISCS DSRLVPELVT QREPGDLFVI 70 80 90 100 110 120 RNAGNIVPSY GPEPGGVSAS VEYAVAALRV SDIVICGHSN CGAMTAIASC QCMDHMPAVS 130 140 150 160 170 180 HWLRYADSAR VVNEARPHSD LPSKAAAMVR ENVIAQLANL QTHPSVRLAL EEGRIALHGW 190 200 210 VYDIESGSIA AFDGATRQFV PLAANPRVCA IPLRQPTAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the cyn operon in Escherichia coli K12." Sung Y.-C., Fuchs J.A. J. Biol. Chem. 263:14769-14775(1988) [PubMed: 3049588] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"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.
[4]	"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]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Carbonic anhydrase in Escherichia coli. A product of the cyn operon." Guilloton M.B., Korte J.J., Lamblin A.-F.J., Fuchs J.A., Anderson P.M. J. Biol. Chem. 267:3731-3734(1992) [PubMed: 1740425] [Abstract] Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 1-20.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M23219 Genomic DNA. Translation: AAA23625.1. U73857 Genomic DNA. Translation: AAB18063.1. U00096 Genomic DNA. Translation: AAC73442.1. AP009048 Genomic DNA. Translation: BAE76121.1.
PIR	QRECTC. C64761.
RefSeq	AP_000991.1. NP_414873.1.
3D structure databases
HSSP	HSSP built from PDB template 1EKJ based on UniProtKB P17067.
ModBase	Search...
Protein-protein interaction databases
STRING	P0ABE9.
Genome annotation databases
GeneID	946548.
GenomeReviews	Gene locus JW0330 in contig AP009048_GR. Gene locus b0339 in contig U00096_GR.
KEGG	ecj:JW0330. eco:b0339.
Organism-specific databases
EchoBASE	EB0173.
EcoGene	EG10176. cynT.
CMR	Search...
Phylogenomic databases
HOGENOM	P0ABE9.
OMA	FVSLADH.
Enzyme and pathway databases
BioCyc	EcoCyc:CARBODEHYDRAT-MON.
Gene expression databases
Genevestigator	P0ABE9.
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...

Entry information

Entry name

CYNT_ECOLI

Accession

Primary (citable) accession number: P0ABE9
Secondary accession number(s): P17582, P78278, Q2MC85

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	October 25, 2005
Last modified:	November 3, 2009
This is version 33 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)