NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Garcia E., Richardson P.;
"Complete sequence of chromosome 2 of Ochrobactrum anthropi ATCC 49188.";
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate (By similarity).
CATALYTIC ACTIVITY: L-aspartate + H₂O + NAD(P)⁺ = oxaloacetate + NH₃ + NAD(P)H.
PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1 .
MISCELLANEOUS: The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia (By similarity).
SIMILARITY: Belongs to the L-aspartate dehydrogenase family.

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

CP000759; ABS17096.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001372925.1; -.

3D structure databases

ModBase

A6X792.

Ontologies

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: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]

Genome annotation databases

GeneID

5381939; -.

GenomeReviews

CP000759_GR; Oant_4396.

KEGG

oan:Oant_4396; -.

CMR

A6X792; Oant_4396.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; NAD; NADP; Oxidoreductase; Pyridine nucleotide biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 268`	`268`	`Probable L-aspartate dehydrogenase.`	`PRO_1000067309`
`ACT_SITE`	`221 221`		`By similarity.`
`BINDING`	`125 125`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`191 191`		`NAD (By similarity).`

Sequence information

Length: 268 AA [This is the length of the unprocessed precursor]

Molecular weight: 27854 Da [This is the MW of the unprocessed precursor]

CRC64: 32BA43AEF0CCFC12 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVSETIVLV GWGAIGKRVA DLLAERKSSV RIGAVAVRDR SASRDRLPAG AVLIENPAEL 

        70         80         90        100        110        120 
AASGASLVVE AAGRPSVLPW GEAALSTGMD FAVSSTSAFV DDALFQRLKD AAAASGAKLI 

       130        140        150        160        170        180 
IPPGALGGID ALSAASRLSI ESVEHRIIKP AKAWAGTQAA QLVPLDEISE ATVFFTDTAR 

       190        200        210        220        230        240 
KAADAFPQNA NVAVITSLAG IGLDRTRVTL VADPAARLNT HEIIAEGDFG RMHLRFENGP 

       250        260 
LATNPKSSEM TALNLVRAIE NRVATTVI

A6X792 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools