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Q50940

- CAH_NEIGO

UniProt

Q50940 - CAH_NEIGO

Protein

Carbonic anhydrase

Gene

cah

Organism
Neisseria gonorrhoeae
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (01 Jan 1998)
      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 sitei92 – 921Proton acceptorBy similarity
    Metal bindingi118 – 1181Zinc; catalytic
    Metal bindingi120 – 1201Zinc; catalytic
    Metal bindingi137 – 1371Zinc; catalytic

    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 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase
    Gene namesi
    Name:cah
    OrganismiNeisseria gonorrhoeae
    Taxonomic identifieri485 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

    Subcellular locationi

    Periplasm Curated

    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 – 2626Add
    BLAST
    Chaini27 – 252226Carbonic anhydrasePRO_0000004266Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 207

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    252
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi37 – 393
    Helixi41 – 433
    Helixi44 – 474
    Helixi49 – 524
    Helixi53 – 564
    Beta strandi76 – 794
    Beta strandi86 – 894
    Beta strandi94 – 974
    Beta strandi104 – 1074
    Beta strandi110 – 12213
    Beta strandi124 – 1274
    Beta strandi133 – 1419
    Beta strandi147 – 15610
    Helixi161 – 1633
    Helixi164 – 1674
    Beta strandi172 – 1787
    Helixi185 – 1884
    Beta strandi195 – 2017
    Beta strandi209 – 21810
    Beta strandi220 – 2223
    Helixi224 – 23411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KOPX-ray1.90A/B30-252[»]
    1KOQX-ray1.90A/B30-252[»]
    ProteinModelPortaliQ50940.
    SMRiQ50940. Positions 30-252.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ50940.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni203 – 2042Substrate binding

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.10.200.10. 1 hit.
    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. 1 hit.
    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.

    Q50940-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRFPRTLPR LTAVLLLACT AFSAAAHGNH THWGYTGHDS PESWGNLSEE    50
    FRLCSTGKNQ SPVNITETVS GKLPAIKVNY KPSMVDVENN GHTIQVNYPE 100
    GGNTLTVNGR TYTLKQFHFH VPSENQIKGR TFPMEAHFVH LDENKQPLVL 150
    AVLYEAGKTN GRLSSIWNVM PMTAGKVKLN QPFDASTLLP KRLKYYRFAG 200
    SLTTPPCTEG VSWLVLKTYD HIDQAQAEKF TRAVGSENNR PVQPLNARVV 250
    IE 252
    Length:252
    Mass (Da):28,085
    Last modified:January 1, 1998 - v2
    Checksum:iE4454A145A0F440F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11152 Genomic DNA. Translation: CAA72038.1.
    U11547 Genomic DNA. Translation: AAA75359.1.
    PIRiC56262.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11152 Genomic DNA. Translation: CAA72038.1 .
    U11547 Genomic DNA. Translation: AAA75359.1 .
    PIRi C56262.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KOP X-ray 1.90 A/B 30-252 [» ]
    1KOQ X-ray 1.90 A/B 30-252 [» ]
    ProteinModelPortali Q50940.
    SMRi Q50940. Positions 30-252.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q50940.

    Family and domain databases

    Gene3Di 3.10.200.10. 1 hit.
    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. 1 hit.
    PROSITEi PS00162. ALPHA_CA_1. 1 hit.
    PS51144. ALPHA_CA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete sequence, expression in Escherichia coli, purification and some properties of carbonic anhydrase from Neisseria gonorrhoeae."
      Chirica L.C., Elleby B., Jonsson B.-H., Lindskog S.
      Eur. J. Biochem. 244:755-760(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
    2. "A promoter associated with the neisserial repeat can be used to transcribe the uvrB gene from Neisseria gonorrhoeae."
      Black C.G., Fyfe J.A.M., Davies J.K.
      J. Bacteriol. 177:1952-1958(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-252.
      Strain: MS11.
    3. "Crystal structure of carbonic anhydrase from Neisseria gonorrhoeae and its complex with the inhibitor acetazolamide."
      Huang S., Xue Y., Sauer-Eriksson E., Chirica L., Lindskog S., Jonsson B.-H.
      J. Mol. Biol. 283:301-310(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-252 IN COMPLEX WITH TINC ION AND INHIBITOR ACETAZOLAMIDE.

    Entry informationi

    Entry nameiCAH_NEIGO
    AccessioniPrimary (citable) accession number: Q50940
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 84 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    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