ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q82UP3


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ARGD_NITEU
Primary accession number Q82UP3
Secondary accession numbers None
Integrated into Swiss-Prot on January 16, 2004
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 43)
Name and origin of the protein
Protein name Acetylornithine aminotransferase
Synonyms ACOAT
EC 2.6.1.11
Gene name
Name: argD
OrderedLocusNames: NE1439
From
Nitrosomonas europaea [TaxID: 915] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales; Nitrosomonadaceae; Nitrosomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 19718 / IFO 14298;
DOI=10.1128/JB.185.9.2759-2773.2003; PubMed=12700255 [NCBI, ExPASy, EBI, Israel, Japan]
Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea.";
J. Bacteriol. 185:2759-2773(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AL954747; CAD85350.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_841480.1; -.
3D structure databases
HSSP P12995; 1QJ3. [HSSP ENTRY / PDB]
ModBase Q82UP3.
Enzyme and pathway databases
BioCyc NEUR228410:NE1439-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003992; Molecular function: acetylornithine transaminase activity (inferred from electronic annotation from HAMAP).
GO:0030170; Molecular function: pyridoxal phosphate binding (inferred from electronic annotation from InterPro).
GO:0006526; Biological process: arginine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01107; -; 1.
PBIL [Tree]
InterPro IPR005814; Aminotrans_3.
IPR004636; ArgD_aminotrans.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
Graphical view of domain structure.
Gene3D G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
PANTHER PTHR11986; Aminotrans_3; 1.
PTHR11986:SF19; ArgD_aminotrans; 1.
Pfam PF00202; Aminotran_3; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00707; argD; 1.
PROSITE PS00600; AA_TRANSFER_CLASS_3; 1.
ProtoNet Q82UP3.
Genome annotation databases
GeneID 1082389; -.
GenomeReviews AL954747_GR; NE1439.
KEGG neu:NE1439; -.
NMPDR fig|228410.1.peg.1379; -.
Phylogenomic databases
HOGENOM Q82UP3; -.
Genome annotation databases
CMR Q82UP3; NE1439.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis; Complete proteome; Cytoplasm; Pyridoxal phosphate; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   393  393     Acetylornithine aminotransferase. PRO_0000112761
BINDING   243   243        Pyridoxal phosphate (covalent) (By similarity). 
Sequence information
Length: 393 AA [This is the length of the unprocessed precursor] Molecular weight: 43074 Da [This is the MW of the unprocessed precursor] CRC64: 9BF3CC7977016064 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSHVMNTYAR LPVTFVKGEG VWLWDDQGNR YLDALSGIAV CGVGHCHPVL VKALCEQVST 

        70         80         90        100        110        120 
LIHTSNVYHI QHQERLADRL TSLSGLEKAF FCNSGAEANE AAIKLARLYG HNQGINLPTI 

       130        140        150        160        170        180 
IVMERSFHGR TMATLTATGN RKTQAGFEPL LTGFVRVPYD DLEAVNKVAA NNREIVAILL 

       190        200        210        220        230        240 
ETYQGEGGVN FPQANYLQGL RRICDQNGWL LMLDEVQCGL GRTGKWFAFQ HSEVMPDAMT 

       250        260        270        280        290        300 
LAKGLGSGVP IGACLAGGKA AEVFKPGNHA STFGGNPLAC RAALTTLDII EQEGLMDNAV 

       310        320        330        340        350        360 
TIGNFMWEEF GRRLQAWQDV LKIRGQGMMI GIELPVPCSE LVPEALKRRV LVNVTSEKVV 

       370        380        390 
RLLPALNMQK AEAEQVVTEV SALITWFLES RVK 

Q82UP3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!