D0C1Y9 (D0C1Y9_9GAMM) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Probable L-aspartate dehydrogenase HAMAP-Rule MF_01265
EC=1.4.1.21 HAMAP-Rule MF_01265

Gene names

Name:	nadX HAMAP-Rule MF_01265
ORF Names:	HMPREF0014_02400 EMBL EEW99277.1

Organism

Acinetobacter sp. RUH2624 EMBL EEW99277.1

Taxonomic identifier

575564 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex › Acinetobacter nosocomialis

Protein attributes

Sequence length	263 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate By similarity. HAMAP-Rule MF_01265
Catalytic activity	L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H. HAMAP-Rule MF_01265
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. HAMAP-Rule MF_01265
Miscellaneous	The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia By similarity. HAMAP-Rule MF_01265
Sequence similarities	Belongs to the L-aspartate dehydrogenase family. HAMAP-Rule MF_01265

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis HAMAP-Rule MF_01265
Ligand	NAD HAMAP-Rule MF_01265 NADP HAMAP-Rule MF_01265
Molecular function	Oxidoreductase HAMAP-Rule MF_01265
Gene Ontology (GO)
Biological_process	NAD biosynthetic process Inferred from electronic annotation. Source: HAMAP NADP catabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	NAD binding Inferred from electronic annotation. Source: HAMAP NADP binding Inferred from electronic annotation. Source: HAMAP aspartate dehydrogenase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	216	1	By similarity HAMAP-Rule MF_01265
	Binding site	120	1	NAD; via amide nitrogen By similarity HAMAP-Rule MF_01265
	Binding site	186	1	NAD By similarity HAMAP-Rule MF_01265

Sequences

	Sequence		Length	Mass (Da)
	D0C1Y9 [UniParc]. Last modified November 24, 2009. Version 1. Checksum: A2F94A128F512144	FASTA	263	27,954
	10 20 30 40 50 60 MKKLMMIGFG AMAAEVYAHL PQDLQLKWIV VPSRSIEKVQ SQVSSDIQVI SDIEQCDGTP 70 80 90 100 110 120 DYVIEVAGQA AVKEHAQKVL AKGWTIGLIS VGTLADSEFL VQLKQTAEKN DAHLHLLAGA 130 140 150 160 170 180 IAGIDGISAA KEGGLQKVTY KGCKSPKSWK GSYAEQLVDL DHVSEPTVFF TGTAREAAMK 190 200 210 220 230 240 FPANANVAAT IALAGLGMDE TMVELTVDPT INKNKHTIVA EGGFGQMTIE LVGVPLPSNP 250 260 KTSTLAALSV IRACRNSVEA IQI

References

[1]

"The Genome Sequence of Acinetobacter sp. strain RUH2624." The Broad Institute Genome Sequencing Platform Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S. , Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C., Dijkshoorn L., Haas B., Nusbaum C., Birren B. Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: RUH2624 EMBL EEW99277.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	GG704514 Genomic DNA. Translation: EEW99277.1.
3D structure databases
ProteinModelPortal	D0C1Y9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EEW99277; EEW99277; HMPREF0014_02400.
PATRIC	24353910. VBIAciSp90504_2366.
Enzyme and pathway databases
UniPathway	UPA00253; UER00456.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_01265. NadX.
InterPro	IPR005106. 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]
Pfam	PF01958. DUF108. 1 hit. PF03447. NAD_binding_3. 1 hit. [Graphical view]
PIRSF	PIRSF005227. Asp_dh_NAD_syn. 1 hit.
ProtoNet	Search...

Entry information

Entry name

D0C1Y9_9GAMM

Accession

Primary (citable) accession number: D0C1Y9

Entry history

Integrated into UniProtKB/TrEMBL:	November 24, 2009
Last sequence update:	November 24, 2009
Last modified:	April 3, 2013
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)