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Protein

Carbonic anhydrase 1

Gene

cynT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

H2CO3 = CO2 + H2O.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi39ZincBy similarity1
Metal bindingi41ZincBy similarity1
Metal bindingi98ZincBy similarity1
Metal bindingi101ZincBy similarity1

GO - Molecular functioni

  • carbonate dehydratase activity Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • zinc ion binding Source: EcoCyc

GO - Biological processi

  • carbon utilization Source: InterPro
  • cyanate catabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:CARBODEHYDRAT-MONOMER.
ECOL316407:JW0330-MONOMER.
MetaCyc:CARBODEHYDRAT-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 1 (EC:4.2.1.11 Publication)
Alternative name(s):
Carbonate dehydratase 1
Gene namesi
Name:cynT1 Publication
Ordered Locus Names:b0339, JW0330
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10176. cynT.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000774591 – 219Carbonic anhydrase 1Add BLAST219

Proteomic databases

PaxDbiP0ABE9.
PRIDEiP0ABE9.

Expressioni

Inductioni

By cyanate.1 Publication

Interactioni

Subunit structurei

Oligomer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4259815. 4 interactors.
DIPiDIP-47965N.
IntActiP0ABE9. 1 interactor.
STRINGi511145.b0339.

Structurei

3D structure databases

ProteinModelPortaliP0ABE9.
SMRiP0ABE9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107B2H. Bacteria.
COG0288. LUCA.
HOGENOMiHOG000125182.
InParanoidiP0ABE9.
KOiK01673.
OMAiNIIICGH.
PhylomeDBiP0ABE9.

Family and domain databases

Gene3Di3.40.1050.10. 1 hit.
InterProiIPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]
PANTHERiPTHR11002. PTHR11002. 1 hit.
PfamiPF00484. Pro_CA. 1 hit.
[Graphical view]
SMARTiSM00947. Pro_CA. 1 hit.
[Graphical view]
SUPFAMiSSF53056. SSF53056. 1 hit.
PROSITEiPS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABE9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKEIIDGFLK FQREAFPKRE ALFKQLATQQ SPRTLFISCS DSRLVPELVT
60 70 80 90 100
QREPGDLFVI RNAGNIVPSY GPEPGGVSAS VEYAVAALRV SDIVICGHSN
110 120 130 140 150
CGAMTAIASC QCMDHMPAVS HWLRYADSAR VVNEARPHSD LPSKAAAMVR
160 170 180 190 200
ENVIAQLANL QTHPSVRLAL EEGRIALHGW VYDIESGSIA AFDGATRQFV
210
PLAANPRVCA IPLRQPTAA
Length:219
Mass (Da):23,764
Last modified:October 25, 2005 - v1
Checksum:i5EB41F125EC4D731
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti174 – 176RIA → GS in AAA23625 (PubMed:3049588).Curated3
Sequence conflicti212P → R in AAA23625 (PubMed:3049588).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23219 Genomic DNA. Translation: AAA23625.1.
U73857 Genomic DNA. Translation: AAB18063.1.
U00096 Genomic DNA. Translation: AAC73442.1.
AP009048 Genomic DNA. Translation: BAE76121.1.
PIRiC64761. QRECTC.
RefSeqiNP_414873.1. NC_000913.3.
WP_000658652.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73442; AAC73442; b0339.
BAE76121; BAE76121; BAE76121.
GeneIDi946548.
KEGGiecj:JW0330.
eco:b0339.
PATRICi32115811. VBIEscCol129921_0347.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23219 Genomic DNA. Translation: AAA23625.1.
U73857 Genomic DNA. Translation: AAB18063.1.
U00096 Genomic DNA. Translation: AAC73442.1.
AP009048 Genomic DNA. Translation: BAE76121.1.
PIRiC64761. QRECTC.
RefSeqiNP_414873.1. NC_000913.3.
WP_000658652.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0ABE9.
SMRiP0ABE9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259815. 4 interactors.
DIPiDIP-47965N.
IntActiP0ABE9. 1 interactor.
STRINGi511145.b0339.

Proteomic databases

PaxDbiP0ABE9.
PRIDEiP0ABE9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73442; AAC73442; b0339.
BAE76121; BAE76121; BAE76121.
GeneIDi946548.
KEGGiecj:JW0330.
eco:b0339.
PATRICi32115811. VBIEscCol129921_0347.

Organism-specific databases

EchoBASEiEB0173.
EcoGeneiEG10176. cynT.

Phylogenomic databases

eggNOGiENOG4107B2H. Bacteria.
COG0288. LUCA.
HOGENOMiHOG000125182.
InParanoidiP0ABE9.
KOiK01673.
OMAiNIIICGH.
PhylomeDBiP0ABE9.

Enzyme and pathway databases

BioCyciEcoCyc:CARBODEHYDRAT-MONOMER.
ECOL316407:JW0330-MONOMER.
MetaCyc:CARBODEHYDRAT-MONOMER.

Miscellaneous databases

PROiP0ABE9.

Family and domain databases

Gene3Di3.40.1050.10. 1 hit.
InterProiIPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]
PANTHERiPTHR11002. PTHR11002. 1 hit.
PfamiPF00484. Pro_CA. 1 hit.
[Graphical view]
SMARTiSM00947. Pro_CA. 1 hit.
[Graphical view]
SUPFAMiSSF53056. SSF53056. 1 hit.
PROSITEiPS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCYNT_ECOLI
AccessioniPrimary (citable) accession number: P0ABE9
Secondary accession number(s): P17582, P78278, Q2MC85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: November 2, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.