N(G),N(G)-dimethylarginine dimethylaminohydrolase 1

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O08557 (DDAH1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 95. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
N(G),N(G)-dimethylarginine dimethylaminohydrolase 1
Short name=DDAH-1
Short name=Dimethylarginine dimethylaminohydrolase 1
EC=3.5.3.18

Alternative name(s):
DDAHI
Dimethylargininase-1

Gene names

Name:	Ddah1
Synonyms:	Ddah

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation. Ref.3
Catalytic activity	N(omega),N(omega)-dimethyl-L-arginine + H₂O = dimethylamine + L-citrulline.
Enzyme regulation	Inhibited by zinc ions. Ref.3
Subunit structure	Monomer By similarity.
Tissue specificity	Detected in red blood cells (at protein level). Widely distributed, high amounts found in kidney, brain, aorta and pancreas. Ref.3
Sequence similarities	Belongs to the DDAH family.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	arginine metabolic process Inferred from direct assay PubMed 17322279. Source: RGD citrulline metabolic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of angiogenesis Inferred from mutant phenotype PubMed 12237779. Source: RGD positive regulation of nitric oxide biosynthetic process Inferred from mutant phenotype PubMed 12237779. Source: RGD regulation of systemic arterial blood pressure Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	amino acid binding Inferred from direct assay PubMed 17322279. Source: RGD dimethylargininase activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 285

284

N(G),N(G)-dimethylarginine dimethylaminohydrolase 1

PRO_0000171120

Sites

Active site

173

Proton donor By similarity

Active site

274

Nucleophile By similarity

Metal binding

274

Zinc By similarity

Binding site

Substrate; via carbonyl oxygen By similarity

Binding site

Substrate By similarity

Binding site

Substrate By similarity

Binding site

Substrate By similarity

Binding site

Substrate By similarity

Binding site

145

Substrate By similarity

Binding site

268

Substrate; via carbonyl oxygen By similarity

Amino acid modifications

Modified residue

N-acetylalanine Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O08557 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9FE8DF56E37A7E4A
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FASTA

285

31,426

        10         20         30         40         50         60 
MAGLSHPSVF GRATHAVVRA PPESLCRHAL RRSQGEEVDF ARAERQHQLY VGVLGSKLGL 

        70         80         90        100        110        120 
QVVQLPADES LPDCVFVEDV AVVCEETALI TRPGAPSRRK EVDMMKEALE KLQLNIVEMK 

       130        140        150        160        170        180 
DENATLDGGD VLFTGREFFV GLSKRTNQRG AEILADTFKD YAVSTVPVAD SLHLKSFCSM 

       190        200        210        220        230        240 
AGPNLIAIGS SESAQKALKI MQQMSDHRYD KLTVPDDMAA NCIYLNIPSK GHVLLHRTPE 

       250        260        270        280 
EYPESAKVYE KLKDHLLIPV SNSEMEKVDG LLTCCSVFIN KKTDS

« Hide

References

[1]	"Cloning and sequencing of cDNA encoding NG,NG-dimethylarginine dimethylaminohydrolase from rat kidney." Kimoto M., Sasakawa T., Tsuji H., Miyatake S., Oka T., Nio N., Ogawa T. Biochim. Biophys. Acta 1337:6-10(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ACETYLATION AT ALA-2. Strain: Wistar. Tissue: Kidney.
[2]	Lubec G., Afjehi-Sadat L., Chen W.-Q. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 46-57; 112-136 AND 160-175, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord.
[3]	"Contribution of whole blood to the control of plasma asymmetrical dimethylarginine." Billecke S.S., Kitzmiller L.A., Northrup J.J., Whitesall S.E., Kimoto M., Hinz A.V., D'Alecy L.G. Am. J. Physiol. 291:H1788-H1796(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D86041 mRNA. Translation: BAA18993.1.
IPI	IPI00231194.
RefSeq	NP_071633.1. NM_022297.2.
UniGene	Rn.7398.
3D structure databases
ProteinModelPortal	O08557.
SMR	O08557. Positions 8-281.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000044971.
PTM databases
PhosphoSite	O08557.
Proteomic databases
PaxDb	O08557.
PRIDE	O08557.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000045016; ENSRNOP00000044971; ENSRNOG00000014613.
GeneID	64157.
KEGG	rno:64157.
Organism-specific databases
CTD	23576.
RGD	70968. Ddah1.
Phylogenomic databases
eggNOG	COG1834.
GeneTree	ENSGT00390000009331.
HOGENOM	HOG000161035.
HOVERGEN	HBG055937.
KO	K01482.
OrthoDB	EOG4320ZN.
Gene expression databases
ArrayExpress	O08557.
Genevestigator	O08557.
GermOnline	ENSRNOG00000014613. Rattus norvegicus.
Family and domain databases
InterPro	IPR003198. Amidino_trans. [Graphical view]
Pfam	PF02274. Amidinotransf. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O08557.
ChEMBL	CHEMBL4196.
NextBio	612794.

Entry information

Entry name

DDAH1_RAT

Accession

Primary (citable) accession number: O08557

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Recent format changes

Overview of recent format changes

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents