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P49900 (ARGI_LITCT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Arginase, hepatic
EC=3.5.3.1
OrganismLithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Taxonomic identifier8400 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Rana › Aquarana

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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
Urea cycle
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological_processarginine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

urea cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 – 323323Arginase, hepatic
PRO_0000173702

Regions

Region127 – 1315Substrate binding By similarity
Region138 – 1403Substrate binding By similarity

Sites

Metal binding1021Manganese 1 By similarity
Metal binding1251Manganese 1 By similarity
Metal binding1251Manganese 2 By similarity
Metal binding1271Manganese 2 By similarity
Metal binding1291Manganese 1 By similarity
Metal binding2331Manganese 1 By similarity
Metal binding2331Manganese 2 By similarity
Metal binding2351Manganese 2 By similarity
Binding site1841Substrate By similarity
Binding site2781Substrate By similarity

Experimental info

Sequence conflict316 – 3216SLRVPD → ICVF in BAA07422. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P49900 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: FD8167DF02C69583

FASTA32335,293
        10         20         30         40         50         60 
MSERTKRSVG VLGAPFSKGQ ARGGVEEGPI YIRRAGLIEK LEELEYEVRD YGDLHFPELP 

        70         80         90        100        110        120 
CDEPFQNVKN PRTVGQAAEK VANAVSEVKR SGRVCLTLGG DHSLAVGTIT GHAKVHPDLC 

       130        140        150        160        170        180 
VVWVDAHADI NTPITSPSGN LHGQPVSFLI RELQTKVPAI PGFSWVQPSL SAKDIVYIGL 

       190        200        210        220        230        240 
RDVDPGEHYI LKTLGIKSYS MSDVDRLTIN KVMEETIEFL VGKKKRPIHL SFDIDGLDPS 

       250        260        270        280        290        300 
VAPATGTPVP GGLTYREGMY ITEQLYNTGL LSAVDMMEVN PSRGETERES KLTVNTSLNM 

       310        320 
ILSCFGKARE GFHASSLRVP DLI

« Hide

References

[1]"Reprogramming of gene expression in the liver of Rana catesbeiana tadpoles during spontaneous and thyroid hormone induced metamorphosis."
Atkinson B.G., Helbing C.C., Chen Y.
(In) Davey K.G., Peter R.E., Tobe S.S. (eds.); Perspectives in comparative endocrinology, pp.416-423, National Research Council of Canada, Ottawa (1994)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Cloning of cDNAs encoding argininosuccinate lyase and arginase from Rana catesbeiana liver and regulation of their mRNAs during spontaneous and thyroid hormone-induced metamorphosis."
Iwase K., Yamauchi K., Ishikawa K.
Biochim. Biophys. Acta 1260:139-146(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U26351 mRNA. Translation: AAA68073.1.
D38303 mRNA. Translation: BAA07422.1.
PIRS52134.

3D structure databases

ProteinModelPortalP49900.
SMRP49900. Positions 7-313.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG003030.

Enzyme and pathway databases

UniPathwayUPA00158; UER00270.

Family and domain databases

Gene3D3.40.800.10. 1 hit.
InterProIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERPTHR11358. PTHR11358. 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_LITCT
AccessionPrimary (citable) accession number: P49900
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 3, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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