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Information on EC 4.2.1.1 - carbonic anhydrase and Organism(s) Arabidopsis thaliana
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4.2.1.1 carbonic anhydraseIUBMB Comments
The enzyme catalyses the reversible hydration of gaseous CO2 to carbonic acid, which dissociates to give hydrogencarbonate above neutral pH. It is widespread and found in archaea, bacteria, and eukaryotes. Three distinct classes exist, and appear to have evolved independently. Contains zinc.
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- 4.2.1.1
- acetazolamide
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- isozymes
- hypoxia
- glaucoma
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intraocular
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tumor-associated
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-
diuretic
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basolateral
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- calcification
- topiramate
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reabsorption
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cotransporter
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electrolyte
-
glut-1
-
branchial
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open-angle
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antiepileptic
-
beta-blockers
- h+-atpase
-
acuity
- hif-1alpha
-
hypotensive
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anticonvulsant
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hypercapnia
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microelectrodes
- amiloride
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cystoid
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thiazide
- medicine
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glaucomatous
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
carbonic anhydrase, ca ix, ca ii, hca ii, hca i, carbonic anhydrase ix, carbonic anhydrase ii, hca ix, ca iv, anhydrase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
anhydrase
-
-
-
-
CA
-
-
-
-
CA-IX
-
-
-
-
CA-VA
-
-
-
-
CA-VB
-
-
-
-
CA-VI
-
-
-
-
CA-VII
-
-
-
-
CA-XII
-
-
-
-
CA-XIV
-
-
-
-
CA1
-
-
-
-
CA2
-
-
-
-
CAIX
-
-
-
-
carbonate anhydrase
-
-
-
-
Carbonate dehydratase
-
-
-
-
Carbonate dehydratase IX
-
-
-
-
Carbonate dehydratase VA
-
-
-
-
Carbonate dehydratase VB
-
-
-
-
Carbonate dehydratase VI
-
-
-
-
Carbonate dehydratase VII
-
-
-
-
Carbonate dehydratase XII
-
-
-
-
Carbonate dehydratase XIV
-
-
-
-
carbonic acid anhydrase
-
-
-
-
carbonic anhydrase
carbonic dehydratase
-
-
-
-
carboxyanhydrase
-
-
-
-
dehydratase, carbonate
-
-
-
-
Membrane antigen MN
-
-
-
-
P54/58N
-
-
-
-
pMW1
-
-
-
-
RCC-associated antigen G250
-
-
-
-
Renal cell carcinoma-associated antigen G250
-
-
-
-
Salivary carbonic anhydrase
-
-
-
-
Secreted carbonic anhydrase
-
-
-
-
Tumor antigen HOM-RCC-3.1.3
-
-
-
-
carbonic anhydrase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
addition
-
-
-
-
elimination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
carbonic acid hydro-lyase (carbon-dioxide-forming)
The enzyme catalyses the reversible hydration of gaseous CO2 to carbonic acid, which dissociates to give hydrogencarbonate above neutral pH. It is widespread and found in archaea, bacteria, and eukaryotes. Three distinct classes exist, and appear to have evolved independently. Contains zinc.
CAS REGISTRY NUMBER
COMMENTARY
9001-03-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
other carbonic anhydrase isoforms than the well-characterized betaCA1 may contribute to the CO2 transfer in the cell to the catalytic site of ribulose 1,5-bisphosphate carboxylase/oxygenase
-
-
?
additional information
?
-
-
other carbonic anhydrase isoforms than the well-characterized betaCA1 may contribute to the CO2 transfer in the cell to the catalytic site of ribulose 1·5-bisphosphate carboxylase/oxygenase
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
other carbonic anhydrase isoforms than the well-characterized betaCA1 may contribute to the CO2 transfer in the cell to the catalytic site of ribulose 1,5-bisphosphate carboxylase/oxygenase
-
-
?
additional information
?
-
-
other carbonic anhydrase isoforms than the well-characterized betaCA1 may contribute to the CO2 transfer in the cell to the catalytic site of ribulose 1·5-bisphosphate carboxylase/oxygenase
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetazolamide
-
at 0.5 mM inhibition of the cabonic anhydrase activity of the high molecular mass protein and stimulation of activity of the low molecular mass carrier in the PSII-membranes. At 0.5 mM acetazolamide moderately inhibits the carbonic anhydrase activity of PSI membranes
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
functional carbonic anhydrase genes are more strongly expressed in green tissue, but strong expression is also found in roots for alphaCA2
-
functional carbonic anhydrase genes are more strongly expressed in green tissue, but strong expression is also found in roots for betaCA3 and betaCA6
-
functional carbonic anhydrase genes are more strongly expressed in green tissue, but strong expression is also found in roots for alphaCA2
-
functional carbonic anhydrase genes are more strongly expressed in green tissue, but strong expression is also found in roots for betaCA3, betaCA6
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
the NADH-ubiquinone oxidoreductase complex (complex I, EC 1.6.5.3) is the main entrance site of electrons into the respiratory chain. In a variety of eukaryotic organisms, except animals and fungi (Opisthokonta), it contains an extra domain comprising trimers of putative gamma-carbonic anhydrases, named the CA domain, which has been proposed to be essential for assembly of complex I. The CA domain of plant complex I contributes to sustaining efficient photosynthesis under ambient (photorespiratory) conditions. The CA protein domain contains at least two different gamma-CA proteins, CA1 (At1g19580) and CA2 (At1g47260), which show conserved active-site regions, and two less well-conserved gamma-CA-like proteins, CAL1 (At5g63510) and CAL2 (At3g48680), containing non-conservative replacements of putatively important amino acids
malfunction
Arabidopsis thaliana mutants defective in two CA subunits show an altered photorespiratory phenotype. Mutants grown in ambient air show growth retardation compared to wild-type plants, a feature that is reversed by cultivating plants in a high-CO2 atmosphere. Under photorespiratory conditions, carbon assimilation is diminished and glycine accumulates, suggesting an imbalance with respect to photorespiration. Additionally, transcript levels of specific CA subunits are reduced in plants grown under non-photorespiratory conditions, leaves of ca2cal1 and ca2cal2 double mutants exhibited increased ROS levels. Mutants ca2cal1 and ca2cal2 show growth retardation in normal air. Mutant phenotypes, overview
malfunction
Arabidopsis thaliana mutants defective in two CA subunits show an altered photorespiratory phenotype. Mutants grown in ambient air show growth retardation compared to wild-type plants, a feature that is reversed by cultivating plants in a high-CO2 atmosphere. Under photorespiratory conditions, carbon assimilation is diminished and glycine accumulates, suggesting an imbalance with respect to photorespiration. Additionally, transcript levels of specific CA subunits are reduced in plants grown under non-photorespiratory conditions. Mutant phenotypes, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ATCA1_ARATH
284
0
32698
Swiss-Prot
Secretory Pathway (Reliability: 1)
ATCA2_ARATH
245
0
28362
Swiss-Prot
Secretory Pathway (Reliability: 1)
ATCA3_ARATH
277
0
31398
Swiss-Prot
Secretory Pathway (Reliability: 2)
ATCA4_ARATH
267
0
30593
Swiss-Prot
Secretory Pathway (Reliability: 2)
ATCA5_ARATH
277
0
32164
Swiss-Prot
Secretory Pathway (Reliability: 1)
ATCA6_ARATH
260
2
29948
Swiss-Prot
Secretory Pathway (Reliability: 1)
ATCA7_ARATH
275
1
31620
Swiss-Prot
Secretory Pathway (Reliability: 1)
ATCA8_ARATH
389
1
42567
Swiss-Prot
Secretory Pathway (Reliability: 5)
BCA1_ARATH
347
0
37450
Swiss-Prot
Chloroplast (Reliability: 1)
BCA2_ARATH
331
0
36615
Swiss-Prot
other Location (Reliability: 5)
BCA3_ARATH
258
0
28829
Swiss-Prot
other Location (Reliability: 2)
BCA4_ARATH
280
0
30836
Swiss-Prot
other Location (Reliability: 3)
BCA5_ARATH
301
0
33401
Swiss-Prot
Chloroplast (Reliability: 2)
BCA6_ARATH
290
0
33072
Swiss-Prot
Mitochondrion (Reliability: 2)
A0A178V4Q8_ARATH
478
0
54326
TrEMBL
Secretory Pathway (Reliability: 1)
A0A654ECN3_ARATH
258
0
28830
TrEMBL
other Location (Reliability: 2)
A0A178W1Y8_ARATH
63
0
6753
TrEMBL
Mitochondrion (Reliability: 5)
A0A7G2ES94_ARATH
273
0
31377
TrEMBL
other Location (Reliability: 3)
A0A178W2Z9_ARATH
121
0
13814
TrEMBL
other Location (Reliability: 1)
A0A5S9XWF4_ARATH
265
1
29979
TrEMBL
Secretory Pathway (Reliability: 1)
A0A178UTI0_ARATH
256
0
27980
TrEMBL
other Location (Reliability: 3)
A0A7G2DV86_ARATH
272
1
31237
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7G2E3Q9_ARATH
278
0
31719
TrEMBL
Mitochondrion (Reliability: 2)
A0A5S9T9F2_ARATH
275
1
31620
TrEMBL
Secretory Pathway (Reliability: 1)
A0A178W457_ARATH
278
1
32027
TrEMBL
Secretory Pathway (Reliability: 1)
A0A178W367_ARATH
120
0
13860
TrEMBL
Chloroplast (Reliability: 3)
A0A654FRB4_ARATH
267
0
30593
TrEMBL
Secretory Pathway (Reliability: 2)
A0A178WEU5_ARATH
145
0
16197
TrEMBL
other Location (Reliability: 3)
A0A7G2DYJ5_ARATH
299
0
33938
TrEMBL
other Location (Reliability: 5)
A0A5S9VRI9_ARATH
258
0
28816
TrEMBL
other Location (Reliability: 2)
A0A7G2E4R2_ARATH
271
0
29982
TrEMBL
other Location (Reliability: 2)
A0A1P8ANM5_ARATH
279
0
31364
TrEMBL
Mitochondrion (Reliability: 2)
Q56X90_ARATH
259
0
28184
TrEMBL
other Location (Reliability: 2)
A0A654FVP3_ARATH
301
0
33401
TrEMBL
Chloroplast (Reliability: 2)
A0A178V525_ARATH
301
0
33383
TrEMBL
Chloroplast (Reliability: 2)
A0A654FRG5_ARATH
247
1
28029
TrEMBL
Secretory Pathway (Reliability: 1)
A0A7G2EFR1_ARATH
276
0
31751
TrEMBL
Secretory Pathway (Reliability: 1)
A0A178W4R2_ARATH
181
0
20338
TrEMBL
other Location (Reliability: 4)
A0A178VK19_ARATH
347
0
37450
TrEMBL
Chloroplast (Reliability: 1)
A0A178UT81_ARATH
259
0
28344
TrEMBL
other Location (Reliability: 2)
A0A1I9LQB3_ARATH
259
0
28198
TrEMBL
other Location (Reliability: 2)
A0A178V615_ARATH
284
0
32698
TrEMBL
Secretory Pathway (Reliability: 1)
A0A654EMR4_ARATH
280
0
30818
TrEMBL
other Location (Reliability: 3)
A0A654EJ93_ARATH
290
0
33070
TrEMBL
Mitochondrion (Reliability: 2)
A0A5S9XKG2_ARATH
286
0
32968
TrEMBL
Secretory Pathway (Reliability: 1)
C0Z272_ARATH
290
0
31348
TrEMBL
Chloroplast (Reliability: 1)
A0A178VW72_ARATH
276
0
31717
TrEMBL
Secretory Pathway (Reliability: 1)
A0A178V4K1_ARATH
267
0
30637
TrEMBL
Secretory Pathway (Reliability: 1)
A0A178VLF2_ARATH
336
0
36144
TrEMBL
Chloroplast (Reliability: 1)
A0A7G2F274_ARATH
267
0
30578
TrEMBL
Secretory Pathway (Reliability: 1)
F4K873_ARATH
330
0
36528
TrEMBL
other Location (Reliability: 5)
F4K875_ARATH
330
0
36486
TrEMBL
other Location (Reliability: 5)
A0A654G125_ARATH
267
0
29336
TrEMBL
other Location (Reliability: 1)
A0A5S9WT29_ARATH
280
0
30836
TrEMBL
other Location (Reliability: 3)
A8MQY4_ARATH
310
0
34426
TrEMBL
other Location (Reliability: 5)
A0A7G2F7L7_ARATH
237
0
25951
TrEMBL
other Location (Reliability: 2)
A0A178W987_ARATH
258
0
28426
TrEMBL
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H216N
additional information
H216N
-
proton shuttle replaced with a residue that does not transfer protons
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Arabidopsis thaliana plant transformation for expression of mutant enzymes via Agrobacterium tumefaciens strain GV3101
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rowlett, R.S.; Tu, C.; McKay, M.M.; Preiss, J.R.; Loomis, R.J.; Hicks, K.A.; Marchione, R.J.; Strong, J.A.; Donovan jr., G.S.; Chamberlin, J.E.
Kinetic characterization of wild-type and proton transfer-impaired variants of beta-carbonic anhydrase from Arabidopsis thaliana
Arch. Biochem. Biophys.
404
197-209
2002
Arabidopsis thaliana
Rowlett, R.S.; Tu, C.; Murray, P.S.; Chamberlin, J.E.
Examination of the role of Gln-158 in the mechanism of CO2 hydration catalyzed by beta-carbonic anhydrase from Arabidopsis thaliana
Arch. Biochem. Biophys.
425
25-32
2004
Arabidopsis thaliana
Tu, C.; Rowlett, R.S.; Tripp, B.C.; Ferry, J.G.; Silverman, D.N.
Chemical rescue of proton transfer in catalysis by carbonic anhydrases in the beta- and gamma-class
Biochemistry
41
15429-15435
2002
Arabidopsis thaliana, Methanosarcina thermophila
Fabre, N.; Reiter, I.M.; Becuwe-Linka, N.; Genty, B.; Rumeau, D.
Characterization and expression analysis of genes encoding alpha and beta carbonic anhydrases in Arabidopsis
Plant Cell Environ.
30
617-629
2007
Arabidopsis thaliana
Ferreira, F.J.; Guo, C.; Coleman, J.R.
Reduction of plastid-localized carbonic anhydrase activity results in reduced Arabidopsis seedling survivorship
Plant Physiol.
147
585-594
2008
Arabidopsis thaliana
Ignatova, L.K.; Rudenko, N.N.; Mudrik, V.A.; Fedorchuk, T.P.; Ivanov, B.N.
Carbonic anhydrase activity in Arabidopsis thaliana thylakoid membrane and fragments enriched with PSI or PSII
Photosynth. Res.
110
89-98
2011
Arabidopsis thaliana
Soto, D.; Cordoba, J.P.; Villarreal, F.; Bartoli, C.; Schmitz, J.; Maurino, V.G.; Braun, H.P.; Pagnussat, G.C.; Zabaleta, E.
Functional characterization of mutants affected in the carbonic anhydrase domain of the respiratory complex I in Arabidopsis thaliana
Plant J.
83
831-844
2015
Arabidopsis thaliana (Q9C6B3), Arabidopsis thaliana (Q9FMV1), Arabidopsis thaliana (Q9FWR5), Arabidopsis thaliana (Q9SMN1), Arabidopsis thaliana
EXTERNAL LINKS (specific for EC-Number 4.2.1.1)
Transporter Classification Database (TCDB): 8.A.164.1.1, 2.A.53.3.12
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