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Protein

Carbonic anhydrase

Gene

NCE103

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible hydration of CO2 to H2CO3. The main role may be to provide inorganic carbon for the bicarbonate-dependent carboxylation reactions catalyzed by pyruvate carboxylase, acetyl-CoA carboxylase and carbamoyl-phosphate synthetase. Involved in protection against oxidative damage. Encodes a substrate for the non-classical protein export pathway for proteins that lack a cleavable signal sequence.5 Publications

Catalytic activityi

H2CO3 = CO2 + H2O.2 Publications

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Kineticsi

kcat is 940000 sec(-1) with CO2 as substrate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi57 – 571Zinc
    Metal bindingi112 – 1121Zinc; via tele nitrogen
    Metal bindingi115 – 1151Zinc

    GO - Molecular functioni

    1. carbonate dehydratase activity Source: SGD
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. carbon utilization Source: InterPro
    2. cellular response to carbon dioxide Source: SGD
    3. cellular response to oxidative stress Source: SGD
    4. metabolic process Source: GOC
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33073-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase
    Non-classical export protein 3
    Gene namesi
    Name:NCE103
    Synonyms:NCE3
    Ordered Locus Names:YNL036W
    ORF Names:N2695
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL036w.
    SGDiS000004981. NCE103.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial intermembrane space Source: SGD
    2. nucleus Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 221221Carbonic anhydrasePRO_0000077468Add
    BLAST

    Proteomic databases

    MaxQBiP53615.
    PaxDbiP53615.
    PeptideAtlasiP53615.

    Expressioni

    Inductioni

    Transcription and activity down-regulated at elevated CO2 concentrations.2 Publications

    Gene expression databases

    GenevestigatoriP53615.

    Interactioni

    Protein-protein interaction databases

    BioGridi35788. 10 interactions.
    DIPiDIP-968N.
    IntActiP53615. 1 interaction.
    MINTiMINT-485874.
    STRINGi4932.YNL036W.

    Structurei

    Secondary structure

    1
    221
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 3518Combined sources
    Helixi37 – 393Combined sources
    Beta strandi51 – 577Combined sources
    Helixi64 – 674Combined sources
    Beta strandi73 – 797Combined sources
    Helixi80 – 823Combined sources
    Helixi89 – 10012Combined sources
    Beta strandi105 – 11410Combined sources
    Helixi116 – 1227Combined sources
    Helixi126 – 1283Combined sources
    Helixi130 – 1323Combined sources
    Helixi135 – 1406Combined sources
    Helixi142 – 1509Combined sources
    Helixi152 – 1554Combined sources
    Helixi161 – 18020Combined sources
    Helixi184 – 1918Combined sources
    Beta strandi196 – 2027Combined sources
    Turni204 – 2063Combined sources
    Beta strandi209 – 2157Combined sources
    Beta strandi217 – 2193Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EYXX-ray2.04A/B14-221[»]
    ProteinModelPortaliP53615.
    SMRiP53615. Positions 17-221.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53615.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0288.
    HOGENOMiHOG000125184.
    InParanoidiP53615.
    OMAiPRFQQVV.
    OrthoDBiEOG7TXKT4.

    Family and domain databases

    Gene3Di3.40.1050.10. 1 hit.
    InterProiIPR001765. Carbonic_anhydrase.
    IPR015892. Carbonic_anhydrase_CS.
    [Graphical view]
    PANTHERiPTHR11002. PTHR11002. 1 hit.
    PfamiPF00484. Pro_CA. 1 hit.
    [Graphical view]
    SMARTiSM00947. Pro_CA. 1 hit.
    [Graphical view]
    SUPFAMiSSF53056. SSF53056. 1 hit.
    PROSITEiPS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P53615-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSATESSSIF TLSHNSNLQD ILAANAKWAS QMNNIQPTLF PDHNAKGQSP
    60 70 80 90 100
    HTLFIGCSDS RYNENCLGVL PGEVFTWKNV ANICHSEDLT LKATLEFAII
    110 120 130 140 150
    CLKVNKVIIC GHTDCGGIKT CLTNQREALP KVNCSHLYKY LDDIDTMYHE
    160 170 180 190 200
    ESQNLIHLKT QREKSHYLSH CNVKRQFNRI IENPTVQTAV QNGELQVYGL
    210 220
    LYNVEDGLLQ TVSTYTKVTP K
    Length:221
    Mass (Da):24,859
    Last modified:October 1, 1996 - v1
    Checksum:i96D0EBAA8BBD9790
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 391L → W in AAC49352 (PubMed:8655575).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U52369 mRNA. Translation: AAC49352.1.
    Z71312 Genomic DNA. Translation: CAA95901.1.
    BK006947 Genomic DNA. Translation: DAA10509.1.
    PIRiS62958.
    RefSeqiNP_014362.3. NM_001182875.3.

    Genome annotation databases

    EnsemblFungiiYNL036W; YNL036W; YNL036W.
    GeneIDi855692.
    KEGGisce:YNL036W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U52369 mRNA. Translation: AAC49352.1.
    Z71312 Genomic DNA. Translation: CAA95901.1.
    BK006947 Genomic DNA. Translation: DAA10509.1.
    PIRiS62958.
    RefSeqiNP_014362.3. NM_001182875.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EYXX-ray2.04A/B14-221[»]
    ProteinModelPortaliP53615.
    SMRiP53615. Positions 17-221.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi35788. 10 interactions.
    DIPiDIP-968N.
    IntActiP53615. 1 interaction.
    MINTiMINT-485874.
    STRINGi4932.YNL036W.

    Chemistry

    BindingDBiP53615.
    ChEMBLiCHEMBL5931.

    Proteomic databases

    MaxQBiP53615.
    PaxDbiP53615.
    PeptideAtlasiP53615.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYNL036W; YNL036W; YNL036W.
    GeneIDi855692.
    KEGGisce:YNL036W.

    Organism-specific databases

    CYGDiYNL036w.
    SGDiS000004981. NCE103.

    Phylogenomic databases

    eggNOGiCOG0288.
    HOGENOMiHOG000125184.
    InParanoidiP53615.
    OMAiPRFQQVV.
    OrthoDBiEOG7TXKT4.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33073-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP53615.
    NextBioi980010.

    Gene expression databases

    GenevestigatoriP53615.

    Family and domain databases

    Gene3Di3.40.1050.10. 1 hit.
    InterProiIPR001765. Carbonic_anhydrase.
    IPR015892. Carbonic_anhydrase_CS.
    [Graphical view]
    PANTHERiPTHR11002. PTHR11002. 1 hit.
    PfamiPF00484. Pro_CA. 1 hit.
    [Graphical view]
    SMARTiSM00947. Pro_CA. 1 hit.
    [Graphical view]
    SUPFAMiSSF53056. SSF53056. 1 hit.
    PROSITEiPS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A new pathway for protein export in Saccharomyces cerevisiae."
      Cleves A.E., Cooper D.N.W., Barondes S.H., Kelly R.B.
      J. Cell Biol. 133:1017-1026(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ATCC 26109 / X2180 / NCYC 826.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Deletion of the carbonic anhydrase-like gene NCE103 of the yeast Saccharomyces cerevisiae causes an oxygen-sensitive growth defect."
      Goetz R., Gnann A., Zimmermann F.K.
      Yeast 15:855-864(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "Complementation of the yeast deletion mutant DeltaNCE103 by members of the beta class of carbonic anhydrases is dependent on carbonic anhydrase activity rather than on antioxidant activity."
      Clark D., Rowlett R.S., Coleman J.R., Klessig D.F.
      Biochem. J. 379:609-615(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Carbonic anhydrase (Nce103p): an essential biosynthetic enzyme for growth of Saccharomyces cerevisiae at atmospheric carbon dioxide pressure."
      Aguilera J., Van Dijken J.P., De Winde J.H., Pronk J.T.
      Biochem. J. 391:311-316(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Physiological and genome-wide transcriptional responses of Saccharomyces cerevisiae to high carbon dioxide concentrations."
      Aguilera J., Petit T., de Winde J.H., Pronk J.T.
      FEMS Yeast Res. 5:579-593(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    10. "The gene NCE103 (YNL036w) from Saccharomyces cerevisiae encodes a functional carbonic anhydrase and its transcription is regulated by the concentration of inorganic carbon in the medium."
      Amoroso G., Morell-Avrahov L., Mueller D., Klug K., Sueltemeyer D.
      Mol. Microbiol. 56:549-558(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION.
    11. "Carbonic anhydrase inhibitors. Inhibition of the beta-class enzyme from the yeast Saccharomyces cerevisiae with anions."
      Isik S., Kockar F., Arslan O., Guler O.O., Innocenti A., Supuran C.T.
      Bioorg. Med. Chem. Lett. 18:6327-6331(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    12. Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "Structural insights into the substrate tunnel of Saccharomyces cerevisiae carbonic anhydrase Nce103."
      Teng Y.B., Jiang Y.L., He Y.X., He W.W., Lian F.M., Chen Y., Zhou C.Z.
      BMC Struct. Biol. 9:67-67(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 14-221.

    Entry informationi

    Entry nameiCAN_YEAST
    AccessioniPrimary (citable) accession number: P53615
    Secondary accession number(s): D6W1E3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: March 4, 2015
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2330 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3

    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 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.