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Protein

Agmatinase, mitochondrial

Gene

Agmat

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Agmatine + H2O = putrescine + urea.

Cofactori

Mn2+PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi168 – 1681Manganese 1PROSITE-ProRule annotation
Metal bindingi193 – 1931Manganese 2PROSITE-ProRule annotation
Metal bindingi284 – 2841Manganese 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_329790. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1923236. Agmat.

Subcellular locationi

  1. Mitochondrion By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3636MitochondrionSequence AnalysisAdd
BLAST
Chaini37 – 358322Agmatinase, mitochondrialPRO_0000320072Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei199 – 1991N6-acetyllysine1 Publication
Modified residuei223 – 2231N6-acetyllysine; alternate1 Publication
Modified residuei223 – 2231N6-succinyllysine; alternate1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiA2AS89.
PaxDbiA2AS89.
PRIDEiA2AS89.

PTM databases

PhosphoSiteiA2AS89.

Expressioni

Tissue specificityi

Detected only in liver.1 Publication

Gene expression databases

BgeeiA2AS89.
CleanExiMM_AGMAT.
ExpressionAtlasiA2AS89. baseline and differential.
GenevestigatoriA2AS89.

Structurei

3D structure databases

ProteinModelPortaliA2AS89.
SMRiA2AS89. Positions 61-355.
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.
InParanoidiA2AS89.
KOiK01480.
OMAiGNDMPRF.
OrthoDBiEOG7M98GH.
PhylomeDBiA2AS89.
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.

A2AS89-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRLLRSSWA RGLGSGVATW RPSAGLFRPG CPGIRQASGA SDTPHHQSPS
60 70 80 90 100
SESPVQPVGV GVCSMMRLPL QSSPEGLDAA FIGVPLDTGT SNRPGARFGP
110 120 130 140 150
CRIREESLML GAVNPSTGAL PFQSLRVADL GNVNVNLYNL QDSCLLIREA
160 170 180 190 200
YQNVLAAGCI PLTLGGDQTI TYPILQAVAK EHGPVGLVHV GAHTNTTDKP
210 220 230 240 250
REEKVYHRTP FRRSVDEGLL DSKRVVQIGI RGSSRTLDPY RYSRSQGFRV
260 270 280 290 300
VLAEDCWMKS LVPLMAEVRQ QMGGKPLYIS FAIDALDPAY APGTGTPEIA
310 320 330 340 350
GLTPSQALEI IRGCQGLNVV GCDLVEVSPP YDLSGNTALL AANLLFEMLC

ALPKVTTV
Length:358
Mass (Da):38,255
Last modified:February 20, 2007 - v1
Checksum:iC98ED338165794B0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451L → R in AAI15694 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL928577 Genomic DNA. Translation: CAM23129.1.
BC115693 mRNA. Translation: AAI15694.1.
CCDSiCCDS38941.1.
RefSeqiNP_001074877.1. NM_001081408.1.
UniGeneiMm.30032.

Genome annotation databases

EnsembliENSMUST00000038161; ENSMUSP00000040853; ENSMUSG00000040706.
GeneIDi75986.
KEGGimmu:75986.
UCSCiuc008vpe.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL928577 Genomic DNA. Translation: CAM23129.1.
BC115693 mRNA. Translation: AAI15694.1.
CCDSiCCDS38941.1.
RefSeqiNP_001074877.1. NM_001081408.1.
UniGeneiMm.30032.

3D structure databases

ProteinModelPortaliA2AS89.
SMRiA2AS89. Positions 61-355.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiA2AS89.

Proteomic databases

MaxQBiA2AS89.
PaxDbiA2AS89.
PRIDEiA2AS89.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038161; ENSMUSP00000040853; ENSMUSG00000040706.
GeneIDi75986.
KEGGimmu:75986.
UCSCiuc008vpe.1. mouse.

Organism-specific databases

CTDi79814.
MGIiMGI:1923236. Agmat.

Phylogenomic databases

eggNOGiCOG0010.
GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204320.
HOVERGENiHBG023165.
InParanoidiA2AS89.
KOiK01480.
OMAiGNDMPRF.
OrthoDBiEOG7M98GH.
PhylomeDBiA2AS89.
TreeFamiTF328612.

Enzyme and pathway databases

UniPathwayiUPA00534; UER00287.
ReactomeiREACT_329790. Agmatine biosynthesis.

Miscellaneous databases

NextBioi344385.
PROiA2AS89.
SOURCEiSearch...

Gene expression databases

BgeeiA2AS89.
CleanExiMM_AGMAT.
ExpressionAtlasiA2AS89. baseline and differential.
GenevestigatoriA2AS89.

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

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "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].
  3. Cited for: TISSUE SPECIFICITY.
  4. "Vertebrate agmatinases: what role do they play in agmatine catabolism?"
    Morris S.M. Jr.
    Ann. N. Y. Acad. Sci. 1009:30-33(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: POTENTIAL LACK OF CATALYTIC ACTIVITY.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199 AND LYS-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSPEB_MOUSE
AccessioniPrimary (citable) accession number: A2AS89
Secondary accession number(s): Q14BN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 20, 2007
Last modified: April 1, 2015
This is version 68 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.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.