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Q5LPG8 (ASPD_SILPO) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Names and origin

Protein namesRecommended name:
Probable L-aspartate dehydrogenase

EC=1.4.1.21
Gene names
Name:nadX
Ordered Locus Names:SPO2880
OrganismSilicibacter pomeroyi [Complete proteome] [HAMAP]
Taxonomic identifier89184 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate By similarity. HAMAP MF_01265

Catalytic activity

L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H. HAMAP MF_01265

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. HAMAP MF_01265

Miscellaneous

The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia By similarity. HAMAP MF_01265

Sequence similarities

Belongs to the L-aspartate dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 275275Probable L-aspartate dehydrogenase HAMAP MF_01265
PRO_0000144892

Sites

Active site2261 By similarity
Binding site1301NAD; via amide nitrogen By similarity
Binding site1961NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5LPG8-1 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: D98084319F319CD8

FASTA27527,808
        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 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000031 Genomic DNA. Translation: AAV96121.1.
RefSeqYP_168088.1.

3D structure databases

ProteinModelPortalQ5LPG8.
SMRQ5LPG8. Positions 14-272.
ModBaseSearch...

Genome annotation databases

GeneID3195767.
GenomeReviewsGene locus SPO2880 in contig CP000031_GR.
KEGGsil:SPO2880.
NMPDRfig|246200.3.peg.3822.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG649642.
OMAECAGHSA.
ProtClustDBPRK13303.

Enzyme and pathway databases

BioCycRPOM246200:SPO_2880-MONOMER.
BRENDA1.4.1.21. 278247.

Family and domain databases

HAMAPMF_01265. NadX.
[Tree]
InterProIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR011182. Asp_DH_NAD_syn.
IPR020626. Asp_DH_NAD_syn_prok.
[Graphical view]
PfamPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFPIRSF005227. Asp_dh_NAD_syn. 1 hit.
ProtoNetSearch...

Entry information

Entry nameASPD_SILPO
AccessionPrimary (citable) accession number: Q5LPG8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: February 1, 2005
Last modified: August 10, 2010
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families