Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Kineticsi

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

Manual assertion based on experiment ini

      Sites

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Metal bindingi57ZincCombined sources1 Publication1
      Metal bindingi59ZincBy similarity1
      Metal bindingi112Zinc; via tele nitrogenCombined sources1 Publication1
      Metal bindingi115ZincCombined sources1 Publication1

      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
      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
      Proteomesi
      • UP000002311 Componenti: Chromosome XIV

      Organism-specific databases

      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

      Pathology & Biotechi

      Chemistry databases

      ChEMBLiCHEMBL5931.

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      ChainiPRO_00000774681 – 221Carbonic anhydraseAdd BLAST221

      Proteomic databases

      MaxQBiP53615.
      PRIDEiP53615.

      Expressioni

      Inductioni

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

      Interactioni

      Protein-protein interaction databases

      BioGridi35788. 8 interactors.
      DIPiDIP-968N.
      IntActiP53615. 1 interactor.
      MINTiMINT-485874.

      Chemistry databases

      BindingDBiP53615.

      Structurei

      Secondary structure

      1221
      Legend: HelixTurnBeta strandPDB Structure known for this area
      Show more details
      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      Helixi18 – 35Combined sources18
      Helixi37 – 39Combined sources3
      Beta strandi51 – 57Combined sources7
      Helixi64 – 67Combined sources4
      Beta strandi73 – 79Combined sources7
      Helixi80 – 82Combined sources3
      Helixi89 – 100Combined sources12
      Beta strandi105 – 114Combined sources10
      Helixi116 – 122Combined sources7
      Helixi126 – 128Combined sources3
      Helixi130 – 132Combined sources3
      Helixi135 – 140Combined sources6
      Helixi142 – 150Combined sources9
      Helixi152 – 155Combined sources4
      Helixi161 – 180Combined sources20
      Helixi184 – 191Combined sources8
      Beta strandi196 – 202Combined sources7
      Turni204 – 206Combined sources3
      Beta strandi209 – 215Combined sources7
      Beta strandi217 – 219Combined sources3

      3D structure databases

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

      Miscellaneous databases

      EvolutionaryTraceiP53615.

      Family & Domainsi

      Sequence similaritiesi

      Phylogenomic databases

      HOGENOMiHOG000125184.
      InParanoidiP53615.
      KOiK01673.
      OMAiTERINEY.
      OrthoDBiEOG092C4AA9.

      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)DescriptionActionsGraphical viewLength
      Sequence conflicti39L → W in AAC49352 (PubMed:8655575).Curated1

      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
      PDB entryMethodResolution (Å)ChainPositionsPDBsum
      3EYXX-ray2.04A/B14-221[»]
      ProteinModelPortaliP53615.
      SMRiP53615.
      ModBaseiSearch...
      MobiDBiSearch...

      Protein-protein interaction databases

      BioGridi35788. 8 interactors.
      DIPiDIP-968N.
      IntActiP53615. 1 interactor.
      MINTiMINT-485874.

      Chemistry databases

      BindingDBiP53615.
      ChEMBLiCHEMBL5931.

      Proteomic databases

      MaxQBiP53615.
      PRIDEiP53615.

      Protocols and materials databases

      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

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

      Organism-specific databases

      EuPathDBiFungiDB:YNL036W.
      SGDiS000004981. NCE103.

      Phylogenomic databases

      HOGENOMiHOG000125184.
      InParanoidiP53615.
      KOiK01673.
      OMAiTERINEY.
      OrthoDBiEOG092C4AA9.

      Enzyme and pathway databases

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

      Miscellaneous databases

      EvolutionaryTraceiP53615.
      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...

      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: November 2, 2016
      This is version 122 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

      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 one 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.