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 Q9HYA4

[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 ASPD_PSEAE
Primary accession number Q9HYA4
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 42)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: PA3505
From
Pseudomonas aeruginosa [TaxID: 287] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
DOI=10.1038/35023079; PubMed=10984043 [NCBI, ExPASy, EBI, Israel, Japan]
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen.";
Nature 406:959-964(2000).
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
AE004091; AAG06893.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G83206; G83206.
RefSeq NP_252195.1; -.
3D structure databases
ModBase Q9HYA4.
Enzyme and pathway databases
BioCyc PAER208964:PA3505-MON; -.
Organism-specific databases
PseudoCAP PA3505; -.
Ontologies
GO
GO:0033735; Molecular function: aspartate dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from HAMAP).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from HAMAP).
GO:0016639; Molecular function: oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor (inferred from electronic annotation from HAMAP).
GO:0009435; Biological process: NAD biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0006742; Biological process: NADP catabolic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_01265; -; 1.
PBIL [Tree]
InterPro IPR005106; Asp/hSer_DHase_NAD-bd.
IPR002811; Asp_DHase.
IPR011182; Asp_DHase_NAD_syn.
Graphical view of domain structure.
Pfam PF01958; DUF108; 1.
PF03447; NAD_binding_3; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF005227; Asp_dh_NAD_syn; 1.
ProDom PD017325; Asp_dh; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS Q9HYA4.
ProtoNet Q9HYA4.
Genome annotation databases
GeneID 879175; -.
GenomeReviews AE004091_GR; PA3505.
KEGG pae:PA3505; -.
NMPDR fig|208964.1.peg.3505; -.
Phylogenomic databases
HOGENOM Q9HYA4; -.
Genome annotation databases
CMR Q9HYA4; PA3505.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   267  267     Probable L-aspartate dehydrogenase. PRO_0000144890
ACT_SITE   220   220        By similarity. 
BINDING   124   124        NAD; via amide nitrogen (By similarity). 
BINDING   190   190        NAD (By similarity). 
Sequence information
Length: 267 AA [This is the length of the unprocessed precursor] Molecular weight: 27920 Da [This is the MW of the unprocessed precursor] CRC64: 208FBC975A872F86 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLNIVMIGCG AIGAGVLELL ENDPQLRVDA VIVPRDSETQ VRHRLASLRR PPRVLSALPA 

        70         80         90        100        110        120 
GERPDLLVEC AGHRAIEQHV LPALAQGIPC LVVSVGALSE PGLVERLEAA AQAGGSRIEL 

       130        140        150        160        170        180 
LPGAIGAIDA LSAARVGGLE SVRYTGRKPA SAWLGTPGET VCDLQRLEKA RVIFDGSARE 

       190        200        210        220        230        240 
AARLYPKNAN VAATLSLAGL GLDRTQVRLI ADPESCENVH QVEASGAFGG FELTLRGKPL 

       250        260 
AANPKTSALT VYSVVRALGN HAHAISI
Q9HYA4 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 au flag APAF Australia Mirror sites: Brazil Canada China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!