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P46512 (CAH1_FLALI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Carbonic anhydrase 1

EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase 1
OrganismFlaveria linearis (Narrowleaf yellowtops)
Taxonomic identifier4225 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceTageteaeFlaveria

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Subunit structure

Homohexamer By similarity.

Subcellular location

Cytoplasm Potential.

Domain

Possesses a transit-like peptide, but it is proposed that this peptide is not removed and that therefore the enzyme stays in the cytoplasm instead of going to the chloroplast By similarity.

Sequence similarities

Belongs to the beta-class carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandZinc
   Molecular functionLyase
Gene Ontology (GO)
   Biological processcarbon utilization

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Carbonic anhydrase 1
PRO_0000077455

Regions

Region1 – 109109Chloroplast transit peptide-like
Compositional bias41 – 477Poly-Ser

Sequences

Sequence LengthMass (Da)Tools
P46512 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 2B71061E73C7E7CD

FASTA33035,574
        10         20         30         40         50         60 
MSTASAFAIN APSFVNASSL KKSSTSSARS GVLSARFTCN SSSSSSSATP PSLIRNEPVF 

        70         80         90        100        110        120 
AAPAPIITPN WTEDGNESYE EAIDALKKML IEKGELEPVA AARIDQITAQ AAAPDTKAPF 

       130        140        150        160        170        180 
DPVERIKSGF VKFKTEKFVT NPALYDELAK GQSPKFMVFA CSDSRVCPSH VLDFQPGEAF 

       190        200        210        220        230        240 
VVRNVANMVP PFDKTKYSGV GAAVEYAVLH LKVQEIFVIG HSRCGGIKGL MTFPDEGPHS 

       250        260        270        280        290        300 
TDFIEDWVKV CLPAKSKVVA EHNGTHLDDQ CVQCEKEAVN VSLGNLLTYP FVRDGLRNNT 

       310        320        330 
LALKGGHYDF VNGTFELWAL DFGLSSPTSV 

« Hide

References

[1]"Molecular comparison of carbonic anhydrase from Flaveria species demonstrating different photosynthetic pathways."
Ludwig M., Burnell J.N.
Plant Mol. Biol. 29:353-365(1995) [PubMed: 7579185] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U19738 mRNA. Translation: AAA86993.1.
PIRS61883.

3D structure databases

ProteinModelPortalP46512.
SMRP46512. Positions 124-330.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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]
SMARTSM00947. Pro_CA. 1 hit.
[Graphical view]
SUPFAMSSF53056. Prok_plnt_COanhd. 1 hit.
PROSITEPS00704. PROK_CO2_ANHYDRASE_1. 1 hit.
PS00705. PROK_CO2_ANHYDRASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAH1_FLALI
AccessionPrimary (citable) accession number: P46512
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 31, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families