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Q9ZK28 (DHAS_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Aspartate-semialdehyde dehydrogenase

Short name=ASA dehydrogenase
Short name=ASADH
EC=1.2.1.11
Alternative name(s):
Aspartate-beta-semialdehyde dehydrogenase
Gene names
Name:asd
Ordered Locus Names:jhp_1114
OrganismHelicobacter pylori (strain J99) (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate By similarity. HAMAP MF_02121

Catalytic activity

L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH. HAMAP MF_02121

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. HAMAP MF_02121

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. HAMAP MF_02121

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. HAMAP MF_02121

Subunit structure

Homodimer By similarity. HAMAP MF_02121

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346Aspartate-semialdehyde dehydrogenase HAMAP MF_02121
PRO_0000141377

Regions

Nucleotide binding12 – 154NADP By similarity
Nucleotide binding40 – 412NADP By similarity
Nucleotide binding161 – 1622NADP By similarity

Sites

Active site1311Acyl-thioester intermediate By similarity
Active site2531Proton acceptor By similarity
Binding site1011Phosphate By similarity
Binding site1581Substrate By similarity
Binding site2251Phosphate By similarity
Binding site2461Substrate By similarity
Binding site3261NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZK28 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 76A7A7C3C4EF6287

FASTA34638,131
        10         20         30         40         50         60 
MKTYNVAIVG ASGAVGQELI KGLENSFFPI KKFVPLASAR SAGKKIRAFN KDYEILETTH 

        70         80         90        100        110        120 
EVFEKEEIDI AFFSAGGSVS EEFAISASKT ALVIDNTSFF RLNKDVPLVV PEINAQEIFN 

       130        140        150        160        170        180 
APLNIIANPN CSTIQMTQIL NPLHLHFKIK SVIVSTYQAV SGAGNKGIES LKNELKTALE 

       190        200        210        220        230        240 
HLEKDPAIDL NQVLQAGAFA YPIAFNAIAH IDTFKENGYT KEELKMVHET HKIMGVDFPI 

       250        260        270        280        290        300 
SATCVRVPVL RSHSESLSIA FEKEFDLKEV YEVLKNAPSV VVCDDPSHNL YPTPLKASHT 

       310        320        330        340 
DSVFIGRLRK DLFDKKTLHG FCVADQLRVG AATNALKIAL HYIKNA 

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed: 9923682] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001439 Genomic DNA. Translation: AAD06695.1.
PIRC71847.
RefSeqNP_223831.1. NC_000921.1.

3D structure databases

ProteinModelPortalQ9ZK28.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9ZK28.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID889756.
GenomeReviewsGene locus jhp_1114 in contig AE001439_GR.
KEGGhpj:jhp1114.
NMPDRfig|85963.1.peg.1109.
PATRIC20607044. VBIHelPyl98156_1210.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0136.
HOGENOMHBG518238.
OMAFHGKQVE.
PhylomeDBQ9ZK28.
ProtClustDBCLSK496405.

Enzyme and pathway databases

BioCycHPYL85963:JHP1114-MONOMER.

Family and domain databases

HAMAPMF_02121. ASADH.
[Tree]
InterProIPR000319. Asp-semialdehyde_DH_CS.
IPR012080. Asp_semialdehyde_DH.
IPR005986. Asp_semialdehyde_DH_beta.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR012280. Semialdhyde_DH_dimer_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00133.
PfamPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
PIRSFPIRSF000148. ASA_dh. 1 hit.
SMARTSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR01296. Asd_B. 1 hit.
PROSITEPS01103. ASD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHAS_HELPJ
AccessionPrimary (citable) accession number: Q9ZK28
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: January 25, 2012
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families