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Reviewed, UniProtKB/Swiss-Prot Q1QBB6 (ASPD_PSYCK)

Last modified January 19, 2010. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable L-aspartate dehydrogenase
    EC=1.4.1.21
Gene names
Name: nadX
Ordered Locus Names: Pcryo_1256
OrganismPsychrobacter cryohalolentis (strain K5) [Complete proteome] [HAMAP]
Taxonomic identifier335284 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length263 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 – 263263Probable L-aspartate dehydrogenase HAMAP MF_01265
PRO_1000067311

Sites

Active site2161 By similarity
Binding site1201NAD; via amide nitrogen By similarity
Binding site1861NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1QBB6-1 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 47927F6132E01CA0

FASTA26327,858
        10         20         30         40         50         60 
MKNVMFIGYG SMARKVHEML PKNIILSTVL VSTRSAEIIK TELGESIAVI TSVDDLIETP 

        70         80         90        100        110        120 
DLAVEMSGQD GLKEHAIKIL GKSIPLGIIS VGAFTDEKFA ISLADTAEAN GVEIHILAGA 

       130        140        150        160        170        180 
VAGIDGIHAA SFAGLSDVVY QGKKHPSSWK GSHADRLIDY DNLVEPTVFF TGTAREAAAL 

       190        200        210        220        230        240 
FPDNSNVAAT IAIAGVGLDD TTVELIADPT LEYNIHHIMA KGVFGKLEIS MAGLPLVENP 

       250        260 
KTSSLAAFSA LRLCCQIDQV IQM 

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References

[1]"Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000323 Genomic DNA. Translation: ABE75037.1.
RefSeqYP_580521.1.

3D structure databases

SMRQ1QBB6. Positions 4-262.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1QBB6.

Genome annotation databases

GeneID4034285.
GenomeReviewsGene locus Pcryo_1256 in contig CP000323_GR.
KEGGpcr:Pcryo_1256.
NMPDRfig|335284.3.peg.838.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1712.
HOGENOMHBG649642.
OMAECAGHSA.

Enzyme and pathway databases

BioCycPCRY335284:PCRYO_1256-MONOMER.

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.
IPR016040. NAD(P)-bd_dom.
[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_PSYCK
AccessionPrimary (citable) accession number: Q1QBB6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 16, 2006
Last modified: January 19, 2010
This is version 29 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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents