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P20507

- CAH1_CHLRE

UniProt

P20507 - CAH1_CHLRE

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Protein

Carbonic anhydrase 1

Gene

CAH1

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei112 – 1121Proton acceptorBy similarity
Metal bindingi163 – 1631Zinc; catalyticBy similarity
Metal bindingi165 – 1651Zinc; catalyticBy similarity
Metal bindingi182 – 1821Zinc; catalyticBy similarity
Binding sitei260 – 2601SubstrateBy similarity

GO - Molecular functioni

  1. carbonate dehydratase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. one-carbon metabolic process Source: InterPro
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

  1. periplasmic space Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 377357Carbonic anhydrase 1PRO_0000004257Add
BLAST
Chaini21 – 305285Carbonic anhydrase 1 large chainPRO_0000004258Add
BLAST
Chaini341 – 37737Carbonic anhydrase 1 small chainPRO_0000004259Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 – 21Interchain1 Publication
Disulfide bondi61 ↔ 2641 Publication
Glycosylationi101 – 1011N-linked (GlcNAc...)1 Publication
Glycosylationi135 – 1351N-linked (GlcNAc...)1 Publication
Disulfide bondi194 ↔ 1981 Publication
Disulfide bondi296 ↔ 351Interchain (between large and small chains)1 Publication
Glycosylationi297 – 2971N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP20507.
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.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 383Combined sources
Turni43 – 486Combined sources
Turni61 – 633Combined sources
Beta strandi70 – 723Combined sources
Helixi74 – 785Combined sources
Helixi87 – 893Combined sources
Beta strandi92 – 943Combined sources
Beta strandi101 – 1099Combined sources
Beta strandi114 – 1207Combined sources
Beta strandi125 – 1339Combined sources
Helixi142 – 1454Combined sources
Beta strandi152 – 16716Combined sources
Beta strandi169 – 1724Combined sources
Beta strandi178 – 18710Combined sources
Helixi192 – 1943Combined sources
Beta strandi198 – 21215Combined sources
Turni215 – 2173Combined sources
Helixi218 – 2214Combined sources
Beta strandi230 – 2334Combined sources
Helixi242 – 2454Combined sources
Beta strandi252 – 2587Combined sources
Beta strandi266 – 27510Combined sources
Beta strandi277 – 2804Combined sources
Helixi281 – 29010Combined sources
Beta strandi293 – 2975Combined sources
Helixi346 – 3483Combined sources
Beta strandi350 – 3556Combined sources
Beta strandi371 – 3744Combined sources

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni260 – 2612Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi307 – 32014His-richAdd
BLAST

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3338.

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. 1 hit.
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

GeneIDi5717875.
KEGGicre:CHLREDRAFT_24120.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90206 Genomic DNA. Translation: BAA14232.2 .
PIRi S14187. A35795.
RefSeqi XP_001692291.1. XM_001692239.1.
UniGenei Cre.3137.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3B1B X-ray 1.88 A/B 1-377 [» ]
ProteinModelPortali P20507.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P20507.
ProMEXi P20507.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5717875.
KEGGi cre:CHLREDRAFT_24120.

Phylogenomic databases

eggNOGi COG3338.

Family and domain databases

Gene3Di 3.10.200.10. 2 hits.
InterProi IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view ]
PANTHERi PTHR18952. PTHR18952. 1 hit.
Pfami PF00194. Carb_anhydrase. 1 hit.
[Graphical view ]
SMARTi SM01057. Carb_anhydrase. 1 hit.
[Graphical view ]
SUPFAMi SSF51069. SSF51069. 2 hits.
PROSITEi PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "cDNA cloning, sequence, and expression of carbonic anhydrase in Chlamydomonas reinhardtii: regulation by environmental CO2 concentration."
    Fukuzawa H., Fujiwara S., Yamamoto Y., Dionisio-Sese M.L., Miyachi S.
    Proc. Natl. Acad. Sci. U.S.A. 87:4383-4387(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "Structure and differential expression of two genes encoding carbonic anhydrase in Chlamydomonas reinhardtii."
    Fujiwara S., Fukuzawa H., Tachiki A., Miyachi S.
    Proc. Natl. Acad. Sci. U.S.A. 87:9779-9783(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Nucleotide sequences of two genes CAH1 and CAH2 which encode carbonic anhydrase polypeptides in Chlamydomonas reinhardtii."
    Fukuzawa H., Fujiwara S., Tachiki A., Miyachi S.
    Nucleic Acids Res. 18:6441-6442(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: IAM C-9.
  4. "Subunit constitution of carbonic anhydrase from Chlamydomonas reinhardtii."
    Kamo T., Shimogawara K., Fukuzawa H., Muto S., Miyachi S.
    Eur. J. Biochem. 192:557-562(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-37 AND 341-377.
  5. "Structural analysis of periplasmic carbonic anhydrase 1 of Chlamydomonas reinhardtii."
    Ishida S., Muto S., Miyachi S.
    Eur. J. Biochem. 214:9-16(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-101; ASN-135 AND ASN-297.

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 26, 2014
This is version 115 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

External Data

Dasty 3