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Q50940 (CAH_NEIGO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Carbonic anhydrase
EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase
Gene names
Name:cah
OrganismNeisseria gonorrhoeae
Taxonomic identifier485 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc.

Subunit structure

Homodimer.

Subcellular location

Periplasm Potential.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMDisulfide bond
   Technical term3D-structure
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626
Chain27 – 252226Carbonic anhydrase
PRO_0000004266

Regions

Region203 – 2042Substrate binding

Sites

Active site921Proton acceptor By similarity
Metal binding1181Zinc; catalytic
Metal binding1201Zinc; catalytic
Metal binding1371Zinc; catalytic

Amino acid modifications

Disulfide bond54 ↔ 207

Secondary structure

1 ....................................... 252
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q50940 [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: E4454A145A0F440F

FASTA25228,085
        10         20         30         40         50         60 
MPRFPRTLPR LTAVLLLACT AFSAAAHGNH THWGYTGHDS PESWGNLSEE FRLCSTGKNQ 

        70         80         90        100        110        120 
SPVNITETVS GKLPAIKVNY KPSMVDVENN GHTIQVNYPE GGNTLTVNGR TYTLKQFHFH 

       130        140        150        160        170        180 
VPSENQIKGR TFPMEAHFVH LDENKQPLVL AVLYEAGKTN GRLSSIWNVM PMTAGKVKLN 

       190        200        210        220        230        240 
QPFDASTLLP KRLKYYRFAG SLTTPPCTEG VSWLVLKTYD HIDQAQAEKF TRAVGSENNR 

       250 
PVQPLNARVV IE

« Hide

References

[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: 9108244] [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: 7721686] [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: 9761692] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-252 IN COMPLEX WITH TINC ION AND INHIBITOR ACETAZOLAMIDE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y11152 Genomic DNA. Translation: CAA72038.1.
U11547 Genomic DNA. Translation: AAA75359.1.
PIRC56262.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KOPX-ray1.90A/B30-252[»]
1KOQX-ray1.90A/B30-252[»]
ProteinModelPortalQ50940.
SMRQ50940. Positions 30-252.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001148. a_carbonic_anhydrase.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHERPTHR18952. Euk_COanhd. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. Euk_COanhd. 1 hit.
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAH_NEIGO
AccessionPrimary (citable) accession number: Q50940
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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