Reviewed, UniProtKB/Swiss-Prot O25801 (DHAS_HELPY)

Names and origin

Protein names

Recommended name:
    Aspartate-semialdehyde dehydrogenase
      Short name=ASA dehydrogenase
      Short name=ASADH
    EC=1.2.1.11

Gene names

Name:	asd
Ordered Locus Names:	HP_1189

Organism

Helicobacter pylori (Campylobacter pylori) [Complete proteome] [HAMAP]

Taxonomic identifier

210 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH.
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the aspartate-semialdehyde dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	diaminopimelate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methionine biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW threonine biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro aspartate-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: EC protein dimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 346	346	Aspartate-semialdehyde dehydrogenase		PRO_0000141376
Sites
	Active site	131	1	Acyl-thioester intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O25801-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: EAF10B9108A72330	FASTA	346	38,116
	10 20 30 40 50 60 MKTYNVAIVG ASGAVGQELI KGLENSFFPI KKFVPLASTR SAGKKIKAFN KDYEILETTH 70 80 90 100 110 120 EVFEREKIDI AFFSAGGSVS EEFATSASKT ALVVDNTSFF RLNKDVPLVV PEINAKEIFN 130 140 150 160 170 180 APLNIIANPN CSTIQMTQIL NPLHLHFKIK SVIVSTYQAV SGAGNKGIES LKNELKTALE 190 200 210 220 230 240 CLEKDPTIDL NQVLQAGAFA YPIAFNAIAH IDTFKENGYT KEELKMLHET HKIMGVDFPI 250 260 270 280 290 300 SATCVRVPVL RSHSESLSIA FEKEFDLKEV YEVLKNAPSV AVCDDPSHNL YPTPLKASHT 310 320 330 340 DSVFIGRLRK DLFDKKTLHG FCVADQLRVG AATNALKIAL HYIKNA

References

[1]

"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C. Nature 388:539-547(1997) [PubMed: 9252185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000511 Genomic DNA. Translation: AAD08235.1.
PIR	E64668.
RefSeq	NP_207980.1.
3D structure databases
HSSP	HSSP built from PDB template 1BRM based on UniProtKB P00353.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:3753N.
Genome annotation databases
GeneID	899951.
GenomeReviews	Gene locus HP_1189 in contig AE000511_GR.
KEGG	hpy:HP1189.
NMPDR	fig|85962.1.peg.1176.
TIGR	HP_1189.
Phylogenomic databases
HOGENOM	O25801.
OMA	O25801. VFYGHAE.
Enzyme and pathway databases
BRENDA	1.2.1.11. 1131.
Family and domain databases
InterPro	IPR000319. Asp-semialdehyde_DH_CS. IPR012080. Asp_semialdehyde_DH. IPR005986. Asp_semialdehyde_DH_bac. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_C. [Graphical view]
Pfam	PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view]
PIRSF	PIRSF000148. ASA_dh. 1 hit.
TIGRFAMs	TIGR01296. asd_B. 1 hit.
PROSITE	PS01103. ASD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHAS_HELPY

Accession

Primary (citable) accession number: O25801

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)