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Protein

Carbonic anhydrase

Gene

cah

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

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei92Proton acceptorBy similarity1
Metal bindingi118Zinc; catalytic1 Publication1
Metal bindingi120Zinc; catalytic1 Publication1
Metal bindingi137Zinc; catalytic1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.1.1 3590

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

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Add BLAST26
ChainiPRO_000000426627 – 252Carbonic anhydraseAdd BLAST226

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 2071 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1252
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi37 – 39Combined sources3
Helixi41 – 43Combined sources3
Helixi44 – 47Combined sources4
Helixi49 – 52Combined sources4
Helixi53 – 56Combined sources4
Beta strandi76 – 79Combined sources4
Beta strandi86 – 89Combined sources4
Beta strandi94 – 97Combined sources4
Beta strandi104 – 107Combined sources4
Beta strandi110 – 122Combined sources13
Beta strandi124 – 127Combined sources4
Beta strandi133 – 141Combined sources9
Beta strandi147 – 156Combined sources10
Helixi161 – 163Combined sources3
Helixi164 – 167Combined sources4
Beta strandi172 – 178Combined sources7
Helixi185 – 188Combined sources4
Beta strandi195 – 201Combined sources7
Beta strandi209 – 218Combined sources10
Beta strandi220 – 222Combined sources3
Helixi224 – 234Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KOPX-ray1.90A/B30-252[»]
1KOQX-ray1.90A/B30-252[»]
ProteinModelPortaliQ50940
SMRiQ50940
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ50940

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 252Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST222

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni203 – 204Substrate binding1 Publication2

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3338 LUCA

Family and domain databases

Gene3Di3.10.200.10, 1 hit
InterProiView protein in InterPro
IPR001148 Carbonic_anhydrase_a
IPR023561 Carbonic_anhydrase_a-class
IPR018338 Carbonic_anhydrase_a-class_CS
IPR036398 Carbonic_anhydrase_a_sf
PANTHERiPTHR18952 PTHR18952, 1 hit
PfamiView protein in Pfam
PF00194 Carb_anhydrase, 1 hit
SMARTiView protein in SMART
SM01057 Carb_anhydrase, 1 hit
SUPFAMiSSF51069 SSF51069, 1 hit
PROSITEiView protein in PROSITE
PS00162 ALPHA_CA_1, 1 hit
PS51144 ALPHA_CA_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q50940-1 [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:
EMBLi
GenBanki
DDBJi
Links Updated
Y11152 Genomic DNA Translation: CAA72038.1
U11547 Genomic DNA Translation: AAA75359.1
PIRiC56262
RefSeqiWP_003688976.1, NZ_NGQH01000022.1

Similar proteinsi

Entry informationi

Entry nameiCAH_NEIGO
AccessioniPrimary (citable) accession number: Q50940
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: March 28, 2018
This is version 106 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure
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Main funding by: National Institutes of Health