NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.;
"Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
Submitted (MAR-2006) 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

CP000323; ABE75037.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_580521.1; -.

3D structure databases

ModBase

Q1QBB6.

Enzyme and pathway databases

BioCyc

PCRY335284:PCRYO_1256-MON; -.

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).
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

Q1QBB6.

Genome annotation databases

GeneID

4034285; -.

GenomeReviews

CP000323_GR; Pcryo_1256.

KEGG

pcr:Pcryo_1256; -.

NMPDR

fig|335284.3.peg.838; -.

Phylogenomic databases

HOGENOM

Q1QBB6; -.

Genome annotation databases

CMR

Q1QBB6; Pcryo_1256.

Other

ProtoNet

Q1QBB6.

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`	`1 263`	`263`	`Probable L-aspartate dehydrogenase.`	`PRO_1000067311`
`ACT_SITE`	`216 216`		`By similarity.`
`BINDING`	`120 120`		`NAD; via amide nitrogen (By similarity).`
`BINDING`	`186 186`		`NAD (By similarity).`

Sequence information

Length: 263 AA [This is the length of the unprocessed precursor]

Molecular weight: 27858 Da [This is the MW of the unprocessed precursor]

CRC64: 47927F6132E01CA0 [This is a checksum on the sequence]

        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

Q1QBB6 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