Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q0D2L3 (SPEB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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:
Agmatinase, mitochondrial

EC=3.5.3.11
Alternative name(s):
Agmatine ureohydrolase
Short name=AUH
Gene names
Name:Agmat
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length353 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Agmatine + H2O = putrescine + urea.

Cofactor

Manganese Potential.

Pathway

Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the arginase family. Agmatinase subfamily.

Caution

May have little or no activity due to the lack of several residues essential for manganese binding and catalytic activity.

Ontologies

Keywords
   Biological processPutrescine biosynthesis
Spermidine biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processputrescine biosynthetic process from arginine

Inferred from electronic annotation. Source: UniProtKB-UniPathway

spermidine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionagmatinase activity

Inferred from electronic annotation. Source: UniProtKB-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

Transit peptide1 – 3333Mitochondrion Potential
Chain34 – 353320Agmatinase, mitochondrial
PRO_0000320073

Sites

Metal binding1631Manganese 1 By similarity
Metal binding1881Manganese 2 By similarity
Metal binding2791Manganese 2 By similarity

Amino acid modifications

Modified residue1941N6-acetyllysine By similarity
Modified residue2181N6-acetyllysine; alternate By similarity
Modified residue2181N6-succinyllysine; alternate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0D2L3 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: E59BC1FECE84735A

FASTA35337,987
        10         20         30         40         50         60 
MLQLLKSSWV RSAGSGVVTW RASAGLFCPG TRQASDTSDT LHHPSPSSES QVQPVRVCSM 

        70         80         90        100        110        120 
MHLPLQSSPE GLDAAFVGVP LDTGTSNRPG ARFGPRRIRE ESLMLGTVNP STGALPFQSL 

       130        140        150        160        170        180 
RVADLGNVNV NLYNLQDSCR LIREAYQNIL ATGCIPLTLG GDHTITYPIL QAVAKEHGPV 

       190        200        210        220        230        240 
GLVHVGAHSN TSDKPLEDKV YHRTPFRRSV DEGLLDSKRV VQIGIRGSSR TLDPYRYSRS 

       250        260        270        280        290        300 
QGFRVVLAED CWMKSLVPLM AEIRQQMGGV PLYISFAIDA LDPAYAPGTG TPEIAGLTPS 

       310        320        330        340        350 
QALEIIRGCQ GLNVVGCDLV EVSPPYDLSG NTALLAANLL FEMLCALPKV TTV 

« Hide

References

[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC091231 mRNA. Translation: AAH91231.1.
BC105628 mRNA. Translation: AAI05629.1.
RefSeqNP_001041650.1. NM_001048185.1.
UniGeneRn.7880.

3D structure databases

ProteinModelPortalQ0D2L3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000016646.

Proteomic databases

PaxDbQ0D2L3.
PRIDEQ0D2L3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000016648; ENSRNOP00000016646; ENSRNOG00000012315.
GeneID298607.
KEGGrno:298607.
UCSCRGD:1308424. rat.

Organism-specific databases

CTD79814.
RGD1308424. Agmat.

Phylogenomic databases

eggNOGCOG0010.
GeneTreeENSGT00530000063082.
HOGENOMHOG000204320.
HOVERGENHBG023165.
InParanoidQ5BK25.
KOK01480.
OMAGATFRRC.
OrthoDBEOG7M98GH.
PhylomeDBQ0D2L3.
TreeFamTF328612.

Enzyme and pathway databases

UniPathwayUPA00534; UER00287.

Gene expression databases

GenevestigatorQ0D2L3.

Family and domain databases

Gene3D3.40.800.10. 1 hit.
InterProIPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
[Graphical view]
PANTHERPTHR11358. PTHR11358. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01230. agmatinase. 1 hit.
PROSITEPS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio644061.
PROQ0D2L3.

Entry information

Entry nameSPEB_RAT
AccessionPrimary (citable) accession number: Q0D2L3
Secondary accession number(s): Q5BK25
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways