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P0C1D9 (DHAS_CORML) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 38. 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
OrganismCorynebacterium melassecola
Taxonomic identifier41643 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length344 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 – 344344Aspartate-semialdehyde dehydrogenase HAMAP MF_02121
PRO_0000236032

Regions

Nucleotide binding10 – 134NADP By similarity
Nucleotide binding38 – 392NADP By similarity
Nucleotide binding161 – 1622NADP By similarity

Sites

Active site1311Acyl-thioester intermediate By similarity
Active site2571Proton acceptor By similarity
Binding site1011Phosphate By similarity
Binding site1581Substrate By similarity
Binding site2281Phosphate By similarity
Binding site2501Substrate By similarity
Binding site3261NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C1D9 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 3933583CE88E41F8

FASTA34436,226
        10         20         30         40         50         60 
MTTIAVVGAT GQVGQVMRTL LEERNFPADT VRFFASPRSA GRKIEFRGTE IEVEDITQAT 

        70         80         90        100        110        120 
EESLKDIDVA LFSAGGTASK QYAPLFAAAG ATVVDNSSAW RKDDEVPLIV SEVNPSDKDS 

       130        140        150        160        170        180 
LVKGIIANPN CTTMAAMPVL KPLHDAAGLV KLHVSSYQAV SGSGLAGVET LAKQVAAVGD 

       190        200        210        220        230        240 
HNVEFVHDGQ AADAGDVGPY VSPIAYNVLP FAGNLVDDGT FETDEEQKLR NESRKILGLP 

       250        260        270        280        290        300 
DLKVSGTCVR VPVFTGHTLT IHAEFDKAIT VEQAQEILGA ASGVKLVDVP TPLAAAGIDE 

       310        320        330        340 
SLVGRIRQDS TVDDNRGLVL VVSGDNLRKG AALNTIQIAE LLVK

« Hide

References

[1]"Multicopy suppression by asd gene and osmotic stress-dependent complementation by heterologous proA in proA mutants."
Serebrijski I., Wojcik F., Reyes O., Leblon G.
J. Bacteriol. 177:7255-7260(1995) [PubMed: 8522535] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 17965 / AS B-4821.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X82928 Genomic DNA. Translation: CAA58101.1.
PIRS49978.

3D structure databases

ProteinModelPortalP0C1D9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
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_CORML
AccessionPrimary (citable) accession number: P0C1D9
Secondary accession number(s): P26511, Q46062
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: December 14, 2011
This is version 38 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

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