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 2

Gene

can

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi42 – 421Zinc
Metal bindingi44 – 441Zinc
Metal bindingi98 – 981Zinc
Metal bindingi101 – 1011Zinc

GO - Molecular functioni

  • carbonate dehydratase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • carbon utilization Source: UniProtKB
  • metabolic process Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.1.1. 2529.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 2 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase 2
Gene namesi
Name:can
Ordered Locus Names:HI_1301
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 229229Carbonic anhydrase 2PRO_0000077467Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi71421.HI1301.

Structurei

Secondary structure

1
229
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 2019Combined sources
Turni21 – 244Combined sources
Helixi25 – 317Combined sources
Beta strandi37 – 426Combined sources
Turni43 – 453Combined sources
Helixi49 – 535Combined sources
Beta strandi59 – 657Combined sources
Helixi66 – 683Combined sources
Helixi75 – 8612Combined sources
Beta strandi92 – 1009Combined sources
Helixi102 – 1087Combined sources
Helixi116 – 12914Combined sources
Helixi131 – 1355Combined sources
Helixi139 – 1413Combined sources
Helixi142 – 15918Combined sources
Helixi162 – 1698Combined sources
Beta strandi175 – 1817Combined sources
Turni183 – 1853Combined sources
Beta strandi188 – 19710Combined sources
Helixi198 – 21215Combined sources
Helixi217 – 2193Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A8CX-ray2.30A/B/C/D/E/F1-229[»]
2A8DX-ray2.20A/B/C/D/E/F1-229[»]
3E1VX-ray2.80A/B1-229[»]
3E1WX-ray2.60A/B1-229[»]
3E24X-ray2.30A/B1-229[»]
3E28X-ray2.50A/B/C/D/E/F1-229[»]
3E2AX-ray2.30A/B/C/D/E/F1-229[»]
3E2WX-ray2.30A/B/C/D/E/F1-229[»]
3E2XX-ray2.55A/B1-229[»]
3E31X-ray2.95A/B1-229[»]
3E3FX-ray2.30A/B1-229[»]
3E3GX-ray2.30A/B/C/D/E/F1-229[»]
3E3IX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L1-229[»]
3MF3X-ray2.50A/B/C/D/E/F1-221[»]
4WAJX-ray2.70A/B1-229[»]
4WAKX-ray2.49A/B1-229[»]
4WAMX-ray2.20A/B1-229[»]
ProteinModelPortaliP45148.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45148.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0288.
KOiK01673.
OMAiCELNVAE.
OrthoDBiEOG6FFSB8.
PhylomeDBiP45148.

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.
PROSITEiPS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P45148-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKIKQLFAN NYSWAQRMKE ENSTYFKELA DHQTPHYLWI GCSDSRVPAE
60 70 80 90 100
KLTNLEPGEL FVHRNVANQV IHTDFNCLSV VQYAVDVLKI EHIIICGHTN
110 120 130 140 150
CGGIHAAMAD KDLGLINNWL LHIRDIWFKH GHLLGKLSPE KRADMLTKIN
160 170 180 190 200
VAEQVYNLGR TSIVKSAWER GQKLSLHGWV YDVNDGFLVD QGVMATSRET
210 220
LEISYRNAIA RLSILDEENI LKKDHLENT
Length:229
Mass (Da):26,250
Last modified:November 1, 1995 - v1
Checksum:i4EB20478BC9EB6C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22946.1.
PIRiF64170.
RefSeqiNP_439452.1. NC_000907.1.
WP_005631770.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22946; AAC22946; HI_1301.
GeneIDi950229.
KEGGihin:HI1301.
PATRICi20191285. VBIHaeInf48452_1353.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22946.1.
PIRiF64170.
RefSeqiNP_439452.1. NC_000907.1.
WP_005631770.1. NC_000907.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A8CX-ray2.30A/B/C/D/E/F1-229[»]
2A8DX-ray2.20A/B/C/D/E/F1-229[»]
3E1VX-ray2.80A/B1-229[»]
3E1WX-ray2.60A/B1-229[»]
3E24X-ray2.30A/B1-229[»]
3E28X-ray2.50A/B/C/D/E/F1-229[»]
3E2AX-ray2.30A/B/C/D/E/F1-229[»]
3E2WX-ray2.30A/B/C/D/E/F1-229[»]
3E2XX-ray2.55A/B1-229[»]
3E31X-ray2.95A/B1-229[»]
3E3FX-ray2.30A/B1-229[»]
3E3GX-ray2.30A/B/C/D/E/F1-229[»]
3E3IX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L1-229[»]
3MF3X-ray2.50A/B/C/D/E/F1-221[»]
4WAJX-ray2.70A/B1-229[»]
4WAKX-ray2.49A/B1-229[»]
4WAMX-ray2.20A/B1-229[»]
ProteinModelPortaliP45148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI1301.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC22946; AAC22946; HI_1301.
GeneIDi950229.
KEGGihin:HI1301.
PATRICi20191285. VBIHaeInf48452_1353.

Phylogenomic databases

eggNOGiCOG0288.
KOiK01673.
OMAiCELNVAE.
OrthoDBiEOG6FFSB8.
PhylomeDBiP45148.

Enzyme and pathway databases

BRENDAi4.2.1.1. 2529.

Miscellaneous databases

EvolutionaryTraceiP45148.

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.
PROSITEiPS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
  2. "Identification of a novel noncatalytic bicarbonate binding site in eubacterial beta-carbonic anhydrase."
    Cronk J.D., Rowlett R.S., Zhang K.Y., Tu C., Endrizzi J.A., Lee J., Gareiss P.C., Preiss J.R.
    Biochemistry 45:4351-4361(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), ZINC-BINDING.

Entry informationi

Entry nameiCAN_HAEIN
AccessioniPrimary (citable) accession number: P45148
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 24, 2015
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.