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Q162H5 (Q162H5_ROSDO) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length260 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. HAMAP MF_01265

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site2131 By similarity HAMAP MF_01265
Binding site1171NAD; via amide nitrogen By similarity HAMAP MF_01265
Binding site1831NAD By similarity HAMAP MF_01265

Sequences

Sequence LengthMass (Da)Tools
Q162H5 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 36B7B959E76A1F88

FASTA26027,170
        10         20         30         40         50         60 
MKIGIIGEGA IGRYVMDQLD RDGRAPVVSL VRPQRLIGAQ DTGMTRVFHV CDLPPGLDLM 

        70         80         90        100        110        120 
VDCAGHAALI EHGAAILKRG IDLVTVSLGA LADQHVEQSL RQAALTGGAQ LHLASGAIGA 

       130        140        150        160        170        180 
LDCLQAARVG GLSAVRYTGR KPPAGWRGSA AQERVDLDML TTAAAHFEGT ARQAARQYPK 

       190        200        210        220        230        240 
NANVAAAVAI AGLGFERTRV TLIADPDVTA NIHEIEASGA FGRFSFRIEG TALPDNPRSS 

       250        260 
ALAAMSVISA IARRRAPVTT 

« Hide

References

[1]"The complete genome sequence of Roseobacter denitrificans reveals a mixotrophic rather than photosynthetic metabolism."
Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K., O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T., Touchman J.W.
J. Bacteriol. 189:683-690(2007) [PubMed: 17098896] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000362 Genomic DNA. Translation: ABG33118.1.
RefSeqYP_683804.1. NC_008209.1.

3D structure databases

ProteinModelPortalQ162H5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ162H5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4195484.
GenomeReviewsGene locus RD1_3642 in contig CP000362_GR.
KEGGrde:RD1_3642.
NMPDRfig|375451.6.peg.3388.
PATRIC23365237. VBIRosDen86677_3484.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1712.
HOGENOMHBG649642.
OMAECAGHSA.
ProtClustDBPRK13303.

Enzyme and pathway databases

BioCycRDEN375451:RD1_3642-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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK06989.
PfamPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFPIRSF005227. Asp_dh_NAD_syn. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ162H5_ROSDO
AccessionPrimary (citable) accession number: Q162H5
Entry history
Integrated into UniProtKB/TrEMBL: July 25, 2006
Last sequence update: July 25, 2006
Last modified: December 14, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)