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Protein

Carbonic anhydrase 1

Gene

CAH1

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei112Proton acceptorPROSITE-ProRule annotation1
Metal bindingi163Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi165Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi182Zinc; catalyticPROSITE-ProRule annotation1
Binding sitei260SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 1 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase 1
Short name:
CA1
Cleaved into the following 2 chains:
Gene namesi
Name:CAH1
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 201 PublicationAdd BLAST20
ChainiPRO_000000425721 – 377Carbonic anhydrase 1Add BLAST357
ChainiPRO_000000425821 – 305Carbonic anhydrase 1 large chainAdd BLAST285
ChainiPRO_0000004259341 – 377Carbonic anhydrase 1 small chainAdd BLAST37

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi21Interchain1 Publication
Disulfide bondi61 ↔ 2641 Publication
Glycosylationi101N-linked (GlcNAc...)1 Publication1
Glycosylationi135N-linked (GlcNAc...)1 Publication1
Disulfide bondi194 ↔ 1981 Publication
Disulfide bondi296 ↔ 351Interchain (between large and small chains)1 Publication
Glycosylationi297N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP20507.
ProMEXiP20507.

Expressioni

Inductioni

Requires light in addition to a decrease in CO2 concentration during growth.

Interactioni

Subunit structurei

Tetramer of two large and two small subunits linked by two disulfide bonds.

Protein-protein interaction databases

STRINGi3055.EDP04241.

Structurei

Secondary structure

1377
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi36 – 38Combined sources3
Turni43 – 48Combined sources6
Turni61 – 63Combined sources3
Beta strandi70 – 72Combined sources3
Helixi74 – 78Combined sources5
Helixi87 – 89Combined sources3
Beta strandi92 – 94Combined sources3
Beta strandi101 – 109Combined sources9
Beta strandi114 – 120Combined sources7
Beta strandi125 – 133Combined sources9
Helixi142 – 145Combined sources4
Beta strandi152 – 167Combined sources16
Beta strandi169 – 172Combined sources4
Beta strandi178 – 187Combined sources10
Helixi192 – 194Combined sources3
Beta strandi198 – 212Combined sources15
Turni215 – 217Combined sources3
Helixi218 – 221Combined sources4
Beta strandi230 – 233Combined sources4
Helixi242 – 245Combined sources4
Beta strandi252 – 258Combined sources7
Beta strandi266 – 275Combined sources10
Beta strandi277 – 280Combined sources4
Helixi281 – 290Combined sources10
Beta strandi293 – 298Combined sources6
Helixi346 – 348Combined sources3
Beta strandi350 – 355Combined sources6
Beta strandi371 – 374Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3B1BX-ray1.88A/B1-377[»]
ProteinModelPortaliP20507.
SMRiP20507.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini38 – 318Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST281

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni260 – 261Substrate bindingBy similarity2

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi307 – 320His-richAdd BLAST14

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated
Contains 1 alpha-carbonic anhydrase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.

Family and domain databases

Gene3Di3.10.200.10. 2 hits.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 2 hits.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 2 hits.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P20507-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARTGALLLV ALALAGCAQA CIYKFGTSPD SKATVSGDHW DHGLNGENWE
60 70 80 90 100
GKDGAGNAWV CKTGRKQSPI NVPQYQVLDG KGSKIANGLQ TQWSYPDLMS
110 120 130 140 150
NGTSVQVINN GHTIQVQWTY NYAGHATIAI PAMHNQTNRI VDVLEMRPND
160 170 180 190 200
AADRVTAVPT QFHFHSTSEH LLAGKIYPLE LHIVHQVTEK LEACKGGCFS
210 220 230 240 250
VTGILFQLDN GPDNELLEPI FANMPSREGT FSNLPAGTTI KLGELLPSDR
260 270 280 290 300
DYVTYEGSLT TPPCSEGLLW HVMTQPQRIS FGQWNRYRLA VGLKECNSTE
310 320 330 340 350
TAADAGHHHH HRRLLHNHAH LEEVPAATSE PKHYFRRVML AESANPDAYT
360 370
CKAVAFGQNF RNPQYANGRT IKLARYH
Length:377
Mass (Da):41,628
Last modified:February 1, 1991 - v1
Checksum:i26500D573313EB3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90206 Genomic DNA. Translation: BAA14232.2.
PIRiS14187. A35795.
RefSeqiXP_001692291.1. XM_001692239.1.
UniGeneiCre.3137.

Genome annotation databases

EnsemblPlantsiEDP04241; EDP04241; CHLREDRAFT_24120.
GeneIDi5717875.
GrameneiEDP04241; EDP04241; CHLREDRAFT_24120.
KEGGicre:CHLREDRAFT_24120.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90206 Genomic DNA. Translation: BAA14232.2.
PIRiS14187. A35795.
RefSeqiXP_001692291.1. XM_001692239.1.
UniGeneiCre.3137.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3B1BX-ray1.88A/B1-377[»]
ProteinModelPortaliP20507.
SMRiP20507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3055.EDP04241.

Proteomic databases

PaxDbiP20507.
ProMEXiP20507.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiEDP04241; EDP04241; CHLREDRAFT_24120.
GeneIDi5717875.
GrameneiEDP04241; EDP04241; CHLREDRAFT_24120.
KEGGicre:CHLREDRAFT_24120.

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.

Family and domain databases

Gene3Di3.10.200.10. 2 hits.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 2 hits.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 2 hits.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAH1_CHLRE
AccessioniPrimary (citable) accession number: P20507
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 2, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.