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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.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi42ZincCombined sources1 Publication1
Metal bindingi44ZincCombined sources1 Publication1
Metal bindingi98Zinc; via tele nitrogenCombined sources1 Publication1
Metal bindingi101ZincCombined sources1 Publication1

GO - Molecular functioni

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

GO - Biological processi

  • carbon utilization Source: UniProtKB
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:4.2.1.11 Publication)
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
Proteomesi
  • UP000000579 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000774671 – 229Carbonic anhydrase 2Add BLAST229

Interactioni

Protein-protein interaction databases

STRINGi71421.HI1301.

Structurei

Secondary structure

1229
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 20Combined sources19
Turni21 – 24Combined sources4
Helixi25 – 31Combined sources7
Beta strandi37 – 42Combined sources6
Turni43 – 45Combined sources3
Helixi49 – 53Combined sources5
Beta strandi59 – 65Combined sources7
Helixi66 – 68Combined sources3
Helixi75 – 86Combined sources12
Beta strandi92 – 100Combined sources9
Helixi102 – 108Combined sources7
Helixi116 – 129Combined sources14
Helixi131 – 135Combined sources5
Helixi139 – 141Combined sources3
Helixi142 – 159Combined sources18
Helixi162 – 169Combined sources8
Beta strandi175 – 181Combined sources7
Turni183 – 185Combined sources3
Beta strandi188 – 197Combined sources10
Helixi198 – 212Combined sources15
Helixi217 – 219Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP45148.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45148.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG41077A9. Bacteria.
COG0288. LUCA.
KOiK01673.
OMAiRASMQDR.
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
PDB 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.
SMRiP45148.
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

eggNOGiENOG41077A9. Bacteria.
COG0288. LUCA.
KOiK01673.
OMAiRASMQDR.
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...

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: November 2, 2016
This is version 105 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

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 one 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.