Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P53615

- CAN_YEAST

UniProt

P53615 - CAN_YEAST

Protein

Carbonic anhydrase

Gene

NCE103

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

      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

      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. 9 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 – 3518
      Helixi37 – 393
      Beta strandi51 – 577
      Helixi64 – 674
      Beta strandi73 – 797
      Helixi80 – 823
      Helixi89 – 10012
      Beta strandi105 – 11410
      Helixi116 – 1227
      Helixi126 – 1283
      Helixi130 – 1323
      Helixi135 – 1406
      Helixi142 – 1509
      Helixi152 – 1554
      Helixi161 – 18020
      Helixi184 – 1918
      Beta strandi196 – 2027
      Turni204 – 2063
      Beta strandi209 – 2157
      Beta strandi217 – 2193

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      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.
      OMAiQIFTHRN.
      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

      MSATESSSIF TLSHNSNLQD ILAANAKWAS QMNNIQPTLF PDHNAKGQSP    50
      HTLFIGCSDS RYNENCLGVL PGEVFTWKNV ANICHSEDLT LKATLEFAII 100
      CLKVNKVIIC GHTDCGGIKT CLTNQREALP KVNCSHLYKY LDDIDTMYHE 150
      ESQNLIHLKT QREKSHYLSH CNVKRQFNRI IENPTVQTAV QNGELQVYGL 200
      LYNVEDGLLQ TVSTYTKVTP K 221
      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:
      EMBL
      GenBank
      DDBJ
      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:
      EMBL
      GenBank
      DDBJ
      Links Updated
      U52369 mRNA. Translation: AAC49352.1 .
      Z71312 Genomic DNA. Translation: CAA95901.1 .
      BK006947 Genomic DNA. Translation: DAA10509.1 .
      PIRi S62958.
      RefSeqi NP_014362.3. NM_001182875.3.

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      Entry Method Resolution (Å) Chain Positions PDBsum
      3EYX X-ray 2.04 A/B 14-221 [» ]
      ProteinModelPortali P53615.
      SMRi P53615. Positions 17-221.
      ModBasei Search...
      MobiDBi Search...

      Protein-protein interaction databases

      BioGridi 35788. 9 interactions.
      DIPi DIP-968N.
      IntActi P53615. 1 interaction.
      MINTi MINT-485874.
      STRINGi 4932.YNL036W.

      Chemistry

      BindingDBi P53615.
      ChEMBLi CHEMBL5931.

      Proteomic databases

      MaxQBi P53615.
      PaxDbi P53615.
      PeptideAtlasi P53615.

      Protocols and materials databases

      Structural Biology Knowledgebase Search...

      Genome annotation databases

      EnsemblFungii YNL036W ; YNL036W ; YNL036W .
      GeneIDi 855692.
      KEGGi sce:YNL036W.

      Organism-specific databases

      CYGDi YNL036w.
      SGDi S000004981. NCE103.

      Phylogenomic databases

      eggNOGi COG0288.
      HOGENOMi HOG000125184.
      OMAi QIFTHRN.
      OrthoDBi EOG7TXKT4.

      Enzyme and pathway databases

      BioCyci YEAST:G3O-33073-MONOMER.

      Miscellaneous databases

      EvolutionaryTracei P53615.
      NextBioi 980010.

      Gene expression databases

      Genevestigatori P53615.

      Family and domain databases

      Gene3Di 3.40.1050.10. 1 hit.
      InterProi IPR001765. Carbonic_anhydrase.
      IPR015892. Carbonic_anhydrase_CS.
      [Graphical view ]
      PANTHERi PTHR11002. PTHR11002. 1 hit.
      Pfami PF00484. Pro_CA. 1 hit.
      [Graphical view ]
      SMARTi SM00947. Pro_CA. 1 hit.
      [Graphical view ]
      SUPFAMi SSF53056. SSF53056. 1 hit.
      PROSITEi PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
      [Graphical view ]
      ProtoNeti Search...

      Publicationsi

      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: October 1, 2014
      This is version 103 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