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Reviewed, UniProtKB/Swiss-Prot P16016 (CAHC_SPIOL)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Carbonic anhydrase, chloroplastic
    EC=4.2.1.1
Alternative name(s):
    Carbonate dehydratase
OrganismSpinacia oleracea (Spinach)
Taxonomic identifier3562 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsCaryophyllalesAmaranthaceaeSpinacia

Protein attributes

Sequence length319 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.

Subunit structure

Homohexamer.

Subcellular location

Plastidchloroplast stroma.

Sequence similarities

Belongs to the beta-class carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandZinc
   Molecular functionLyase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processcarbon utilization

Inferred from electronic annotation. Source: InterPro

   Cellular componentchloroplast stroma

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: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 9898Chloroplast Ref.2 Ref.3
Chain99 – 319221Carbonic anhydrase, chloroplastic
PRO_0000004271

Experimental info

Sequence conflict991E → G AA sequence Ref.3
Sequence conflict2221F → S in AAA34026. Ref.2
Sequence conflict3111Y → F in AAA34026. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P16016-1 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: 2229B19F02423EEF

FASTA31934,570
        10         20         30         40         50         60 
MSTINGCLTS ISPSRTQLKN TSTLRPTFIA NSRVNPSSSV PPSLIRNQPV FAAPAPIITP 

        70         80         90        100        110        120 
TLKEDMAYEE AIAALKKLLS EKGELENEAA SKVAQITSEL ADGGTPSASY PVQRIKEGFI 

       130        140        150        160        170        180 
KFKKEKYEKN PALYGELSKG QAPKFMVFAC SDSRVCPSHV LDFQPGEAFM VRNIANMVPV 

       190        200        210        220        230        240 
FDKDKYAGVG AAIEYAVLHL KVENIVVIGH SACGGIKGLM SFPDAGPTTT DFIEDWVKIC 

       250        260        270        280        290        300 
LPAKHKVLAE HGNATFAEQC THCEKEAVNV SLGNLLTYPF VRDGLVKKTL ALQGGYYDFV 

       310 
NGSFELWGLE YGLSPSQSV 

« Hide

References

[1]"Spinach carbonic anhydrase primary structure deduced from the sequence of a cDNA clone."
Fawcett T.W., Browse J.A., Volokita M., Bartlett S.G.
J. Biol. Chem. 265:5414-5417(1990) [PubMed: 2108138] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Hybrid 424.
[2]"Spinach chloroplastic carbonic anhydrase: nucleotide sequence analysis of cDNA."
Burnell J.N., Gibbs M.J., Mason J.G.
Plant Physiol. 92:37-40(1990) [PubMed: 16667262] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-319, PROTEIN SEQUENCE OF 99-118.
[3]"Origins and molecular evolution of the carbonic anhydrase isozymes."
Hewett-Emmett D., Hopkins P.J., Tashian R.E., Czelusniak J.
Ann. N. Y. Acad. Sci. 429:338-358(1984) [PubMed: 6430173] [Abstract]
Cited for: PROTEIN SEQUENCE OF 99-118.

Cross-references

Sequence databases

J05403 mRNA. Translation: AAA34027.1.
M27295 mRNA. Translation: AAA34026.1.
PIRA35163.

3D structure databases

HSSPHSSP built from PDB template 1EKJ based on UniProtKB P17067.
SMRP16016. Positions 113-319.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.2.1.1. 286.

Family and domain databases

InterProIPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]
Gene3DG3DSA:3.40.1050.10. CO_anhd_prok_pln. 1 hit.
PANTHERPTHR11002. Carbonic_anhydrase. 1 hit.
PfamPF00484. Pro_CA. 1 hit.
[Graphical view]
PROSITEPS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAHC_SPIOL
AccessionPrimary (citable) accession number: P16016
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: August 1, 1990
Last modified: June 16, 2009
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents