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P20507

- CAH1_CHLRE

UniProt

P20507 - CAH1_CHLRE

Protein

Carbonic anhydrase 1

Gene

CAH1

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Reversible hydration of carbon dioxide.

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.

    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

    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-SubCell

    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 – 383
    Turni43 – 486
    Turni61 – 633
    Beta strandi70 – 723
    Helixi74 – 785
    Helixi87 – 893
    Beta strandi92 – 943
    Beta strandi101 – 1099
    Beta strandi114 – 1207
    Beta strandi125 – 1339
    Helixi142 – 1454
    Beta strandi152 – 16716
    Beta strandi169 – 1724
    Beta strandi178 – 18710
    Helixi192 – 1943
    Beta strandi198 – 21215
    Turni215 – 2173
    Helixi218 – 2214
    Beta strandi230 – 2334
    Helixi242 – 2454
    Beta strandi252 – 2587
    Beta strandi266 – 27510
    Beta strandi277 – 2804
    Helixi281 – 29010
    Beta strandi293 – 2975
    Helixi346 – 3483
    Beta strandi350 – 3556
    Beta strandi371 – 3744

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MARTGALLLV ALALAGCAQA CIYKFGTSPD SKATVSGDHW DHGLNGENWE    50
    GKDGAGNAWV CKTGRKQSPI NVPQYQVLDG KGSKIANGLQ TQWSYPDLMS 100
    NGTSVQVINN GHTIQVQWTY NYAGHATIAI PAMHNQTNRI VDVLEMRPND 150
    AADRVTAVPT QFHFHSTSEH LLAGKIYPLE LHIVHQVTEK LEACKGGCFS 200
    VTGILFQLDN GPDNELLEPI FANMPSREGT FSNLPAGTTI KLGELLPSDR 250
    DYVTYEGSLT TPPCSEGLLW HVMTQPQRIS FGQWNRYRLA VGLKECNSTE 300
    TAADAGHHHH HRRLLHNHAH LEEVPAATSE PKHYFRRVML AESANPDAYT 350
    CKAVAFGQNF RNPQYANGRT IKLARYH 377
    Length:377
    Mass (Da):41,628
    Last modified:February 1, 1991 - v1
    Checksum:i26500D573313EB3D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 113 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