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Protein

Agmatinase, mitochondrial

Gene

AGMAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Agmatine + H2O = putrescine + urea.1 Publication

Cofactori

Mn2+PROSITE-ProRule annotation

Pathway:iputrescine biosynthesis via agmatine pathway

This protein is involved in step 1 of the subpathway that synthesizes putrescine from agmatine.
Proteins known to be involved in this subpathway in this organism are:
  1. Agmatinase, mitochondrial (AGMAT)
This subpathway is part of the pathway putrescine biosynthesis via agmatine pathway, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes putrescine from agmatine, the pathway putrescine biosynthesis via agmatine pathway and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi162 – 1621Manganese 1PROSITE-ProRule annotation
Metal bindingi185 – 1851Manganese 1PROSITE-ProRule annotation
Metal bindingi185 – 1851Manganese 2PROSITE-ProRule annotation
Metal bindingi187 – 1871Manganese 2PROSITE-ProRule annotation
Metal bindingi189 – 1891Manganese 1PROSITE-ProRule annotation
Metal bindingi276 – 2761Manganese 1PROSITE-ProRule annotation
Metal bindingi276 – 2761Manganese 2PROSITE-ProRule annotation
Metal bindingi278 – 2781Manganese 2PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Putrescine biosynthesis, Spermidine biosynthesis

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS04051-MONOMER.
BRENDAi3.5.3.11. 2681.
ReactomeiREACT_14800. 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18407. AGMAT.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24619.

Polymorphism and mutation databases

BioMutaiAGMAT.
DMDMi126302602.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionSequence AnalysisAdd
BLAST
Chaini36 – 352317Agmatinase, mitochondrialPRO_0000002089Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei193 – 1931N6-acetyllysineBy similarity
Modified residuei217 – 2171N6-acetyllysine; alternateBy similarity
Modified residuei217 – 2171N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9BSE5.
PaxDbiQ9BSE5.
PeptideAtlasiQ9BSE5.
PRIDEiQ9BSE5.

PTM databases

PhosphoSiteiQ9BSE5.

Expressioni

Tissue specificityi

Highly expressed in liver and kidney. Also found in skeletal muscle, fetal liver, brain, testis, skin and the gastrointestinal tract. Within brain, expression is higher in the cerebral cortex with lower levels in the medulla and spinal cord.2 Publications

Gene expression databases

BgeeiQ9BSE5.
CleanExiHS_AGMAT.
ExpressionAtlasiQ9BSE5. baseline and differential.
GenevisibleiQ9BSE5. HS.

Organism-specific databases

HPAiHPA026443.
HPA028321.

Interactioni

Protein-protein interaction databases

BioGridi122909. 11 interactions.
STRINGi9606.ENSP00000364986.

Structurei

3D structure databases

ProteinModelPortaliQ9BSE5.
SMRiQ9BSE5. Positions 42-349.
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.
InParanoidiQ9BSE5.
KOiK01480.
OMAiKPDYSLY.
OrthoDBiEOG7M98GH.
PhylomeDBiQ9BSE5.
TreeFamiTF328612.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01230. agmatinase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9BSE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRLLASGCA RGPGPGVGAR PAAGLFHPGR RQSRQASDAP RNQPPSPEFV
60 70 80 90 100
ARPVGVCSMM RLPVQTSPEG LDAAFIGVPL DTGTSNRPGA RFGPRRIREE
110 120 130 140 150
SVMLGTVNPS TGALPFQSLM VADLGDVNVN LYNLQDSCRR IQEAYEKIVA
160 170 180 190 200
AGCIPLTLGG DHTITYPILQ AMAKKHGPVG LLHVDAHTDT TDKALGEKLY
210 220 230 240 250
HGAPFRRCVD EGLLDCKRVV QIGIRGSSTT LDPYRYNRSQ GFRVVLAEDC
260 270 280 290 300
WMKSLVPLMG EVRQQMGGKP IYISFDIDAL DPAYAPGTGT PEIAGLTPSQ
310 320 330 340 350
ALEIIRGCQG LNVMGCDLVE VSPPYDLSGN TALLAANLLF EMLCALPKVT

TV
Length:352
Mass (Da):37,660
Last modified:February 20, 2007 - v2
Checksum:i394738202353314A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451Y → C in BAB15633 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051G → R.3 Publications
Corresponds to variant rs6429757 [ dbSNP | Ensembl ].
VAR_023485
Natural varianti140 – 1401R → Q.1 Publication
Corresponds to variant rs11580170 [ dbSNP | Ensembl ].
VAR_048332

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY057097 mRNA. Translation: AAL24446.1.
AK027037 mRNA. Translation: BAB15633.1.
AL121992 Genomic DNA. Translation: CAI22366.1.
BC005090 mRNA. Translation: AAH05090.1.
CCDSiCCDS160.1.
RefSeqiNP_079034.3. NM_024758.4.
UniGeneiHs.461532.

Genome annotation databases

EnsembliENST00000375826; ENSP00000364986; ENSG00000116771.
GeneIDi79814.
KEGGihsa:79814.
UCSCiuc001awv.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY057097 mRNA. Translation: AAL24446.1.
AK027037 mRNA. Translation: BAB15633.1.
AL121992 Genomic DNA. Translation: CAI22366.1.
BC005090 mRNA. Translation: AAH05090.1.
CCDSiCCDS160.1.
RefSeqiNP_079034.3. NM_024758.4.
UniGeneiHs.461532.

3D structure databases

ProteinModelPortaliQ9BSE5.
SMRiQ9BSE5. Positions 42-349.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122909. 11 interactions.
STRINGi9606.ENSP00000364986.

PTM databases

PhosphoSiteiQ9BSE5.

Polymorphism and mutation databases

BioMutaiAGMAT.
DMDMi126302602.

Proteomic databases

MaxQBiQ9BSE5.
PaxDbiQ9BSE5.
PeptideAtlasiQ9BSE5.
PRIDEiQ9BSE5.

Protocols and materials databases

DNASUi79814.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375826; ENSP00000364986; ENSG00000116771.
GeneIDi79814.
KEGGihsa:79814.
UCSCiuc001awv.2. human.

Organism-specific databases

CTDi79814.
GeneCardsiGC01M015898.
H-InvDBHIX0000155.
HGNCiHGNC:18407. AGMAT.
HPAiHPA026443.
HPA028321.
neXtProtiNX_Q9BSE5.
PharmGKBiPA24619.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0010.
GeneTreeiENSGT00530000063082.
HOGENOMiHOG000204320.
HOVERGENiHBG023165.
InParanoidiQ9BSE5.
KOiK01480.
OMAiKPDYSLY.
OrthoDBiEOG7M98GH.
PhylomeDBiQ9BSE5.
TreeFamiTF328612.

Enzyme and pathway databases

UniPathwayiUPA00534; UER00287.
BioCyciMetaCyc:HS04051-MONOMER.
BRENDAi3.5.3.11. 2681.
ReactomeiREACT_14800. Agmatine biosynthesis.

Miscellaneous databases

GeneWikiiAgmatinase.
GenomeRNAii79814.
NextBioi69414.
PROiQ9BSE5.

Gene expression databases

BgeeiQ9BSE5.
CleanExiHS_AGMAT.
ExpressionAtlasiQ9BSE5. baseline and differential.
GenevisibleiQ9BSE5. HS.

Family and domain databases

Gene3Di3.40.800.10. 1 hit.
InterProiIPR005925. Agmatinase-rel.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERiPTHR11358. PTHR11358. 1 hit.
PfamiPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFiPIRSF036979. Arginase. 1 hit.
PRINTSiPR00116. ARGINASE.
TIGRFAMsiTIGR01230. agmatinase. 1 hit.
PROSITEiPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus."
    Mistry S.K., Burwell T.J., Chambers R.M., Rudolph-Owen L., Spaltmann F., Cook W.J., Morris S.M. Jr.
    Am. J. Physiol. 282:G375-G381(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS ARG-105 AND GLN-140.
    Tissue: Kidney.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-105.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANT ARG-105.
    Tissue: Ovary.
  5. Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSPEB_HUMAN
AccessioniPrimary (citable) accession number: Q9BSE5
Secondary accession number(s): Q5TDH1, Q9H5J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: February 20, 2007
Last modified: June 24, 2015
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. 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.