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UniProtKB/Swiss-Prot entry Q5LPG8

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

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Entry information
Entry name ASPD_SILPO
Primary accession number Q5LPG8
Secondary accession numbers None
Integrated into Swiss-Prot on August 16, 2005
Sequence was last modified on February 1, 2005 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 30)
Name and origin of the protein
Protein name Probable L-aspartate dehydrogenase
Synonym EC 1.4.1.21
Gene name
Name: nadX
OrderedLocusNames: SPO2880
From
Silicibacter pomeroyi [TaxID: 89184] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; Rhodobacteraceae; Silicibacter.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
DOI=10.1038/nature03170; PubMed=15602564 [NCBI, ExPASy, EBI, Israel, Japan]
Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
"Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment.";
Nature 432:910-913(2004).
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
CP000031; AAV96121.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_168088.1; -.
3D structure databases
ModBase Q5LPG8.
Enzyme and pathway databases
BioCyc SPOM246200:SPO_2880-MON; -.
Ontologies
GO
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).
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 Q5LPG8.
Genome annotation databases
GeneID 3195767; -.
GenomeReviews CP000031_GR; SPO2880.
KEGG sil:SPO2880; -.
NMPDR fig|246200.3.peg.3822; -.
Phylogenomic databases
HOGENOM Q5LPG8; -.
Genome annotation databases
CMR Q5LPG8; SPO2880.
Other
ProtoNet Q5LPG8.
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   275  275     Probable L-aspartate dehydrogenase. PRO_0000144892
ACT_SITE   226   226        By similarity. 
BINDING   130   130        NAD; via amide nitrogen (By similarity). 
BINDING   196   196        NAD (By similarity). 
Sequence information
Length: 275 AA [This is the length of the unprocessed precursor] Molecular weight: 27808 Da [This is the MW of the unprocessed precursor] CRC64: D98084319F319CD8 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MWKLWGSWPE GDRVRIALIG HGPIAAHVAA HLPVGVQLTG ALCRPGRDDA ARAALGVSVA 

        70         80         90        100        110        120 
QALEGLPQRP DLLVDCAGHS GLRAHGLTAL GAGVEVLTVS VGALADAVFC AELEDAARAG 

       130        140        150        160        170        180 
GTRLCLASGA IGALDALAAA AMGTGLQVTY TGRKPPQGWR GSRAEKVLDL KALTGPVTHF 

       190        200        210        220        230        240 
TGTARAAAQA YPKNANVAAA VALAGAGLDA TRAELIADPG AAANIHEIAA EGAFGRFRFQ 

       250        260        270 
IEGLPLPGNP RSSALTALSL LAALRQRGAA IRPSF
Q5LPG8 in FASTA format

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