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Q50940

- CAH_NEIGO

UniProt

Q50940 - CAH_NEIGO

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Protein

Carbonic anhydrase

Gene

cah

Organism
Neisseria gonorrhoeae
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
Complete GO annotation...

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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPRFPRTLPR LTAVLLLACT AFSAAAHGNH THWGYTGHDS PESWGNLSEE
60 70 80 90 100
FRLCSTGKNQ SPVNITETVS GKLPAIKVNY KPSMVDVENN GHTIQVNYPE
110 120 130 140 150
GGNTLTVNGR TYTLKQFHFH VPSENQIKGR TFPMEAHFVH LDENKQPLVL
160 170 180 190 200
AVLYEAGKTN GRLSSIWNVM PMTAGKVKLN QPFDASTLLP KRLKYYRFAG
210 220 230 240 250
SLTTPPCTEG VSWLVLKTYD HIDQAQAEKF TRAVGSENNR PVQPLNARVV

IE
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 29, 2014
This is version 85 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