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Q5BCC5 (CAN_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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
EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase
Gene names
ORF Names:AN1805
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible hydration of CO2 to H2CO3. The main role may be to provide inorganic carbon for the bicarbonate-dependent carboxylation reactions catalyzed by pyruvate carboxylase, acetyl-CoA carboxylase and carbamoyl-phosphate synthetase By similarity. Involved in osmoadaptation.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Induction

Down-regulated when grown with elevated levels of potassium chloride. Ref.3

Sequence similarities

Belongs to the beta-class carbonic anhydrase family.

Sequence caution

The sequence CBF85595.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence EAA64970.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processStress response
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcarbon utilization

Inferred from electronic annotation. Source: InterPro

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 228228Carbonic anhydrase
PRO_0000363403

Sites

Metal binding561Zinc By similarity
Metal binding581Zinc By similarity
Metal binding1121Zinc By similarity
Metal binding1151Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5BCC5 [UniParc].

Last modified February 10, 2009. Version 2.
Checksum: 38A7957EDEA4744E

FASTA22825,485
        10         20         30         40         50         60 
MPDPSDRKAV TRYLEQTHDK IFESNRAWVA SKKGADPEFF NKLAAGQSPE YLYIGCSDSR 

        70         80         90        100        110        120 
VPANEIMGLD AGEVFVHRNI ANVVPTIDLS SMSVINYAVG HLKVKHIVVC GHYNCGGVQA 

       130        140        150        160        170        180 
ALTPTDLGIL NPWLRNIRDV YRLHEKELDA IEDDGERFNR LVELNVIESC RSVIKTAVVQ 

       190        200        210        220 
QSYEENGFPI VHGWVFNLKD GLLKDLNIDF PGILADIQKI YNLTKGSS

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed: 19146970] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"Proteome map of Aspergillus nidulans during osmoadaptation."
Kim Y., Nandakumar M.P., Marten M.R.
Fungal Genet. Biol. 44:886-895(2007) [PubMed: 17258477] [Abstract]
Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AACD01000029 Genomic DNA. Translation: EAA64970.1. Sequence problems.
BN001307 Genomic DNA. Translation: CBF85595.1. Different initiation.
RefSeqXP_659409.1. XM_654317.1.

3D structure databases

HSSPHSSP built from PDB template 1I6P based on UniProtKB P61517.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2874926.
KEGGani:AN1805.2.

Phylogenomic databases

OrthoDBEOG4C2MKH.
PhylomeDBQ5BCC5.

Family and domain databases

InterProIPR001765. Carbonic_anhydrase.
IPR015892. Carbonic_anhydrase_CS.
[Graphical view]
Gene3DG3DSA:3.40.1050.10. CO_anhd_prok_pln. 1 hit.
KOK01672.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAN_EMENI
AccessionPrimary (citable) accession number: Q5BCC5
Secondary accession number(s): C8VPG4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 44 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents