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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

      • carbonate dehydratase activity Source: SGD
      • zinc ion binding Source: InterPro

      GO - Biological processi

      • carbon utilization Source: InterPro
      • cellular response to carbon dioxide Source: SGD
      • cellular response to oxidative stress Source: SGD
      • metabolic process Source: GOC
      Complete GO annotation...

      Keywords - Molecular functioni

      Lyase

      Keywords - Ligandi

      Metal-binding, Zinc

      Enzyme and pathway databases

      BioCyciYEAST:G3O-33073-MONOMER.
      BRENDAi4.2.1.1. 984.

      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 Componenti: Chromosome XIV

      Organism-specific databases

      CYGDiYNL036w.
      EuPathDBiFungiDB:YNL036W.
      SGDiS000004981. NCE103.

      Subcellular locationi

      GO - Cellular componenti

      • mitochondrial intermembrane space Source: SGD
      • 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

      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.
      KOiK01673.
      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.
      EuPathDBiFungiDB:YNL036W.
      SGDiS000004981. NCE103.

      Phylogenomic databases

      eggNOGiCOG0288.
      HOGENOMiHOG000125184.
      InParanoidiP53615.
      KOiK01673.
      OMAiPRFQQVV.
      OrthoDBiEOG7TXKT4.

      Enzyme and pathway databases

      BioCyciYEAST:G3O-33073-MONOMER.
      BRENDAi4.2.1.1. 984.

      Miscellaneous databases

      EvolutionaryTraceiP53615.
      NextBioi980010.
      PROiP53615.

      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: June 24, 2015
      This is version 110 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.