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Protein

Agmatinase, mitochondrial

Gene

Agmat

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Agmatine + H2O = putrescine + urea.

Cofactori

Mn2+PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi163 – 1631Manganese 1PROSITE-ProRule annotation
Metal bindingi188 – 1881Manganese 2PROSITE-ProRule annotation
Metal bindingi279 – 2791Manganese 2PROSITE-ProRule annotation

GO - Molecular functioni

  1. agmatinase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. putrescine biosynthetic process from arginine Source: UniProtKB-UniPathway
  2. spermidine biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Putrescine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_287206. Agmatine biosynthesis.
UniPathwayiUPA00534; UER00287.

Names & Taxonomyi

Protein namesi
Recommended name:
Agmatinase, mitochondrial (EC:3.5.3.11)
Alternative name(s):
Agmatine ureohydrolase
Short name:
AUH
Gene namesi
Name:Agmat
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi1308424. Agmat.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionSequence AnalysisAdd
BLAST
Chaini34 – 353320Agmatinase, mitochondrialPRO_0000320073Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941N6-acetyllysineBy similarity
Modified residuei218 – 2181N6-acetyllysine; alternateBy similarity
Modified residuei218 – 2181N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ0D2L3.
PRIDEiQ0D2L3.

Expressioni

Gene expression databases

GenevestigatoriQ0D2L3.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016646.

Structurei

3D structure databases

ProteinModelPortaliQ0D2L3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arginase family. Agmatinase subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0010.
GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204320.
HOVERGENiHBG023165.
InParanoidiQ0D2L3.
KOiK01480.
OMAiGNDMPRF.
OrthoDBiEOG7M98GH.
PhylomeDBiQ0D2L3.
TreeFamiTF328612.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01230. agmatinase. 1 hit.
PROSITEiPS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q0D2L3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLQLLKSSWV RSAGSGVVTW RASAGLFCPG TRQASDTSDT LHHPSPSSES
60 70 80 90 100
QVQPVRVCSM MHLPLQSSPE GLDAAFVGVP LDTGTSNRPG ARFGPRRIRE
110 120 130 140 150
ESLMLGTVNP STGALPFQSL RVADLGNVNV NLYNLQDSCR LIREAYQNIL
160 170 180 190 200
ATGCIPLTLG GDHTITYPIL QAVAKEHGPV GLVHVGAHSN TSDKPLEDKV
210 220 230 240 250
YHRTPFRRSV DEGLLDSKRV VQIGIRGSSR TLDPYRYSRS QGFRVVLAED
260 270 280 290 300
CWMKSLVPLM AEIRQQMGGV PLYISFAIDA LDPAYAPGTG TPEIAGLTPS
310 320 330 340 350
QALEIIRGCQ GLNVVGCDLV EVSPPYDLSG NTALLAANLL FEMLCALPKV

TTV
Length:353
Mass (Da):37,987
Last modified:October 17, 2006 - v1
Checksum:iE59BC1FECE84735A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC091231 mRNA. Translation: AAH91231.1.
BC105628 mRNA. Translation: AAI05629.1.
RefSeqiNP_001041650.1. NM_001048185.1.
UniGeneiRn.7880.

Genome annotation databases

EnsembliENSRNOT00000016648; ENSRNOP00000016646; ENSRNOG00000012315.
GeneIDi298607.
KEGGirno:298607.
UCSCiRGD:1308424. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC091231 mRNA. Translation: AAH91231.1.
BC105628 mRNA. Translation: AAI05629.1.
RefSeqiNP_001041650.1. NM_001048185.1.
UniGeneiRn.7880.

3D structure databases

ProteinModelPortaliQ0D2L3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016646.

Proteomic databases

PaxDbiQ0D2L3.
PRIDEiQ0D2L3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000016648; ENSRNOP00000016646; ENSRNOG00000012315.
GeneIDi298607.
KEGGirno:298607.
UCSCiRGD:1308424. rat.

Organism-specific databases

CTDi79814.
RGDi1308424. Agmat.

Phylogenomic databases

eggNOGiCOG0010.
GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204320.
HOVERGENiHBG023165.
InParanoidiQ0D2L3.
KOiK01480.
OMAiGNDMPRF.
OrthoDBiEOG7M98GH.
PhylomeDBiQ0D2L3.
TreeFamiTF328612.

Enzyme and pathway databases

UniPathwayiUPA00534; UER00287.
ReactomeiREACT_287206. Agmatine biosynthesis.

Miscellaneous databases

NextBioi644061.
PROiQ0D2L3.

Gene expression databases

GenevestigatoriQ0D2L3.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01230. agmatinase. 1 hit.
PROSITEiPS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.

Entry informationi

Entry nameiSPEB_RAT
AccessioniPrimary (citable) accession number: Q0D2L3
Secondary accession number(s): Q5BK25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 17, 2006
Last modified: April 1, 2015
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.