Skip Header

Contribute Send feedback
Read comments (?) or add your own

O67716 (DHAS_AQUAE) 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:aq_1866
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length340 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 – 340340Aspartate-semialdehyde dehydrogenase HAMAP MF_02121
PRO_0000141359

Regions

Nucleotide binding11 – 144NADP By similarity
Nucleotide binding39 – 402NADP By similarity
Nucleotide binding161 – 1622NADP By similarity

Sites

Active site1311Acyl-thioester intermediate By similarity
Active site2451Proton acceptor By similarity
Binding site1001Phosphate By similarity
Binding site1581Substrate By similarity
Binding site2161Phosphate By similarity
Binding site2381Substrate By similarity
Binding site3181NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
O67716 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 5B2172ABA2AC190D

FASTA34037,799
        10         20         30         40         50         60 
MGYRVAIVGA TGEVGRTFLK VLEERNFPVD ELVLYASERS EGKVLTFKGK EYTVKALNKE 

        70         80         90        100        110        120 
NSFKGIDIAL FSAGGSTSKE WAPKFAKDGV VVIDNSSAWR MDPDVPLVVP EVNPEDVKDF 

       130        140        150        160        170        180 
KKKGIIANPN CSTIQMVVAL KPIYDKAGIK RVVVSTYQAV SGAGAKAIED LKNQTKAWCE 

       190        200        210        220        230        240 
GKEMPKAQKF PHQIAFNALP HIDVFFEDGY TKEENKMLYE TRKIMHDENI KVSATCVRIP 

       250        260        270        280        290        300 
VFYGHSESIS METEKEISPE EAREVLKNAP GVIVIDNPQN NEYPMPIMAE GRDEVFVGRI 

       310        320        330        340 
RKDRVFEPGL SMWVVADNIR KGAATNAVQI AELLVKEGLI

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000657 Genomic DNA. Translation: AAC07674.1.
PIRB70461.
RefSeqNP_214284.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67716.
SMRO67716. Positions 2-338.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1193523.
GenomeReviewsGene locus aq_1866 in contig AE000657_GR.
KEGGaae:aq_1866.
NMPDRfig|224324.1.peg.1299.
PATRIC20960694. VBIAquAeo85532_1448.

Phylogenomic databases

HOGENOMHBG518238.
OMADNSSTWR.
PhylomeDBO67716.
ProtClustDBCLSK2299852.

Enzyme and pathway databases

BioCycAAEO224324:AQ_1866-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_AQUAE
AccessionPrimary (citable) accession number: O67716
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents