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PEC Original Annotations
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|
Essentiality
|
|
Class
|
non-essential
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|
References (PMID)
|
|
|
Deletion
|
9-1
(LD)
,
DE(gpt-lac)5
,
DE(argF-lac)169
,
OCR36,37-6 (LD 9C::Ap)
(D)
|
|
Related gene (W3110 PEC)
|
|
Gene Search
|
Search MG1655 PEC by gene name:
cynT
|
|
Related strains
|
|
Strains Search
|
Search strains by gene name:
cynT
Search strains by all related name:
cynT b0339 ECK0336 JW0330
|
General information (Go to Linear View: )
|
|
Gene Name
|
cynT
|
|
Alternative name
|
b0339,ECK0336,JW0330
|
|
Location, Length
|
358,023 - 358,682
(
+
)
;
7.72
min
;
660
(bp) ,
219
(aa)
|
|
Product
|
carbonic anhydrase
|
|
Operon Name
|
cynTSX
|
|
Note
|
GO_component: GO:0005737 - cytoplasm; GO_process: GO:0009440 - cyanate catabolic process; GO_process: GO:0006805 - xenobiotic metabolic process
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Function
|
enzyme; Central intermediary metabolism: Pool, multipurpose conversions
|
|
Gene Ontology
|
GO:0004089
;
carbonate dehydratase activity ( cynT )
GO:0008270
;
zinc ion binding ( cynT )
GO:0015976
;
carbon utilization ( cynT )
GO:0016829
;
lyase activity ( cynT )
GO:0046872
;
metal ion binding ( cynT )
|
|
PID
|
1786534
|
EC number
(KEGG Pathway)
|
4.2.1.1
|
|
Verified Protein Starts
(data
compiled from literature and appropriate citations are available from EcoGene)
|
|
EcoGene
|
cynT
(
EG10176
)
|
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Number of removed
|
0 aa cleaved
|
|
SWISS-PROT
(
Show simple
)
|
Entry name(Acc.no)
|
CYNT_ECOLI
(
P17582
;
P78278
)
|
|
- Protein name
|
Carbonic anhydrase 1
|
|
- Synonyms
|
EC 4.2.1.1
|
|
- Gene name
|
Name=cynT; OrderedLocusNames=b0339, z0435, ECs0392;
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- 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:H(2)CO(3) = CO(2) + H(2)O.
COFACTOR:Binds 1 zinc ion per molecule.
SUBUNIT:Oligomer.
INDUCTION:By cyanate.
SIMILARITY:Belongs to the plant and prokaryotic carbonic anhydrase family.
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Homology Analysis
|
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BLAST
|
|
Bacteria
|
|
GTOP
|
cynT
(
homologous genes of other bacterias
)
|
|
PDB
(database updated :
2007.02.20
)
|
|
PSI-BLAST
|
Chain A, Haemophilus Influenzae Beta-Carbonic Anhydrase
|
|
SWISS-PROT
(database updated :
2007.02.20
)
|
|
BLAST
|
Carbonic anhydrase 1
|
|
PSI-BLAST
|
Carbonic anhydrase 1
|
|
nr
(database updated :
2007.02.20
)
|
|
BLAST
|
carbonic anhydrase [Escherichia coli O157:H7 EDL933]
|
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Pfam 28.0
(database updated :
2015-05
)
|
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Pfam
|
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PROSITE
|
|
PROSITE
|
PKC_PHOSPHO_SITE
CK2_PHOSPHO_SITE
MYRISTYL
PROKAR_LIPOPROTEIN
PROK_CO2_ANHYDRASE_1
PROK_CO2_ANHYDRASE_2
|
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MMBR References
|
FEMS Microbiol Rev. 1990;7(3-4):247-52.
The cyanase operon and cyanate metabolism.
Anderson PM, Sung YC, Fuchs JA.
(
2094285
)
|
J Bacteriol. 1993;175:1443-1451
A physiological role for cyanate-induced carbonic anhydrase in Escherichia coli.
Guilloton, M. B., A. F. Lamblin, E. I. Kozliak, M. Gerami-Nejad, C. Tu, D. Silverman, P. M. Anderson, and J. A. Fuchs.
|
J Biol Chem. 1993;267:3731-3734
Carbonic anhydrase in Escherichia coli: a product of the cyn operon.
Guilloton, M. B., J. J. Korte, A. F. Lamblin, J. A. Fuchs, and P. M. Anderson.
|
J Bacteriol. 1994;176:5711-5717
Expression of proteins encoded by the Escherichia coli cyn operon: carbon dioxide-enhanced degradation of carbonic anhydrase.
Kozliak, E. I., M. B. Guilloton, M. Gerami-Nejad, J. A. Fuchs, and P. M. Anderson.
|
J Bacteriol. 1987;169(6):2639-42.
Identification, mapping, and cloning of the gene encoding cyanase in Escherichia coli K-12.
Sung YC, Parsell D, Anderson PM, Fuchs JA.
(
3034861
)
|
J Biol Chem. 1988;263:14769-14775
Characterization of the cyn operon in Escherichia coli K12.
Sung, Y.-C., and J. A. Fuchs.
|
J Bacteriol. 1987;169(11):5224-30.
Characterization of high-level expression and sequencing of the Escherichia coli K-12 cynS gene encoding cyanase.
Sung YC, Anderson PM, Fuchs JA.
(
2822670
)
|
| Sequences |
Amino acid
FASTA format
|
0001 MKEIIDGFLK FQREAFPKRE ALFKQLATQQ SPRTLFISCS DSRLVPELVT QREPGDLFVI RNAGNIVPSY
0071 GPEPGGVSAS VEYAVAALRV SDIVICGHSN CGAMTAIASC QCMDHMPAVS HWLRYADSAR VVNEARPHSD
0141 LPSKAAAMVR ENVIAQLANL QTHPSVRLAL EEGRIALHGW VYDIESGSIA AFDGATRQFV PLAANPRVCA
0211 IPLRQPTAA
|
Nucleotide
FASTA format
View sequence out neighbor 100bp
|
-100 TATAAGTAAA TCCAATGGAA CTCATCATAA
-070 ATGAGACTTT TACCTTATGA CAATCGGCGA GTAGTCTGCC TCTCATTCCA GAGACAGACA GAGGTTAACG
0001 gtgaaagaga ttattgatgg attccttaaa ttccagcgcg aggcatttcc gaagcgggaa gccttgttta
0071 aacagctggc gacacagcaa agcccgcgca cactttttat ctcctgctcc gacagccgtc tggtccctga
0141 gctggtgacg caacgtgagc ctggcgatct gttcgttatt cgcaacgcgg gcaatatcgt cccttcctac
0211 gggccggaac ccggtggcgt ttctgcttcg gtggagtatg ccgtcgctgc gcttcgggta tctgacattg
0281 tgatttgtgg tcattccaac tgtggcgcga tgaccgccat tgccagctgt cagtgcatgg accatatgcc
0351 tgccgtctcc cactggctgc gttatgccga ttcagcccgc gtcgttaatg aggcgcgccc gcattccgat
0421 ttaccgtcaa aagctgcggc gatggtacgt gaaaacgtca ttgctcagtt ggctaatttg caaactcatc
0491 catcggtgcg cctggcgctc gaagaggggc ggatcgccct gcacggctgg gtctacgaca ttgaaagcgg
0561 cagcatcgca gcttttgacg gcgcaacccg ccagtttgtg ccactggccg ctaatcctcg cgtttgtgcc
0631 ataccgctac gccaaccgac cgcagcgtaa CCTTATTTTT AAACCATCAG GAGTTCCACC ATGATTCAGT
0701 CACAAATTAA CCGCAATATT CGTCTTGATC TTGCCGATGC CATTTTGCTC AGCAAAGCTA
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