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Q12611 (ARGI_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginase

EC=3.5.3.1
Gene names
Name:agaA
ORF Names:AN2901
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaeEmericella

Protein attributes

Sequence length324 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

L-arginine + H2O = L-ornithine + urea.

Cofactor

Binds 2 manganese ions per subunit By similarity.

Pathway

Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.

Subunit structure

Homotrimer By similarity.

Sequence similarities

Belongs to the arginase family.

Ontologies

Keywords
   Biological processArginine metabolism
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processarginine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionarginase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 324324Arginase
PRO_0000173708

Regions

Region145 – 1495Substrate binding By similarity
Region156 – 1583Substrate binding By similarity

Sites

Metal binding1151Manganese 1 By similarity
Metal binding1431Manganese 1 By similarity
Metal binding1431Manganese 2 By similarity
Metal binding1451Manganese 2 By similarity
Metal binding1471Manganese 1 By similarity
Metal binding2491Manganese 1 By similarity
Metal binding2491Manganese 2 By similarity
Metal binding2511Manganese 2 By similarity
Binding site2021Substrate By similarity
Binding site2941Substrate By similarity

Experimental info

Sequence conflict351E → V in AAB05775. Ref.1
Sequence conflict711I → V in AAB05775. Ref.1
Sequence conflict861A → G in AAB05775. Ref.1
Sequence conflict951S → R in AAB05775. Ref.1
Sequence conflict1321Missing in AAB05775. Ref.1
Sequence conflict2581A → V in AAB05775. Ref.1
Sequence conflict2721R → C in AAB05775. Ref.1
Sequence conflict3001E → V in AAB05775. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q12611 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 5767BEB9D7987A16

FASTA32435,479
        10         20         30         40         50         60 
MTSPSTIKQR FLSKPNQLGV VAVGFNGGQC KLGVEAAPMA LVEAGLLDQL RDDLDYEIHY 

        70         80         90        100        110        120 
DNTVHYYEKE IPAEDPDHRG MKKPRAVSAV TETLSSQVYE HSKEGKFTLT LGGDHSIAIG 

       130        140        150        160        170        180 
SISGIAKATR ERLGREIGVI WVDAHADINI PEMSPSGNIH GMPMAFLTRL ATEEKKDIFG 

       190        200        210        220        230        240 
WLQEEHKVNL RKLVYIGLRD VDRGEKKLLR EHGIKAFSMH DVDRHGIGRV VEMALAHIGN 

       250        260        270        280        290        300 
DTPIHLSFDV DALDPQWAPS TGTPVRGGLT LREGDFICEC VHETGNLISM DLVEVNPSLE 

       310        320 
AVGASDTIRT GCSLVRSALG DTLL 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the arginase coding gene and its transcript in Aspergillus nidulans."
Borsuk P., Dzikowska A., Empel J., Grzelak A., Grzeskowiak R., Weglenski P.
Acta Biochim. Pol. 46:391-403(1999) [PubMed: 10547040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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.
[3]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U62482 Genomic DNA. Translation: AAB05775.1.
AACD01000051 Genomic DNA. Translation: EAA63472.1.
BN001306 Genomic DNA. Translation: CBF83783.1.
RefSeqXP_660505.1. XM_655413.1.

3D structure databases

ProteinModelPortalQ12611.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ12611.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00010188; CADANIAP00010188; CADANIAG00010188.
GeneID2873985.
KEGGani:AN2901.2.

Phylogenomic databases

OMAHADINIP.
OrthoDBEOG432471.
PhylomeDBQ12611.

Family and domain databases

InterProIPR014033. Arginase_subgr.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
Gene3DG3DSA:3.40.800.10. Ureohydrolase. 1 hit.
KOK01476.
PANTHERPTHR11358:SF2. Arginase_sub. 1 hit.
PTHR11358. Ureohydrolase. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01229. RocF_arginase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGI_EMENI
AccessionPrimary (citable) accession number: Q12611
Secondary accession number(s): C8VJ82, Q5B979
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 2007
Last modified: January 25, 2012
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families