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Q92IJ0 (DHAS_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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:RC0430
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length338 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-Rule MF_02121

Catalytic activity

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

Pathway

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

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

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_02121

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 338338Aspartate-semialdehyde dehydrogenase HAMAP-Rule MF_02121
PRO_0000280938

Regions

Nucleotide binding13 – 164NADP By similarity
Nucleotide binding41 – 422NADP By similarity
Nucleotide binding162 – 1632NADP By similarity

Sites

Active site1321Acyl-thioester intermediate By similarity
Active site2441Proton acceptor By similarity
Binding site1011Phosphate By similarity
Binding site1591Substrate By similarity
Binding site1871NADP; via carbonyl oxygen By similarity
Binding site2161Phosphate By similarity
Binding site2371Substrate By similarity
Binding site3171NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92IJ0 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: ACADBDF54967BB16

FASTA33837,292
        10         20         30         40         50         60 
MTKKYNIAVI GATGNVGRET LNILAERNFP INKVYAIASD SSLGREVSFG EKILQINSLK 

        70         80         90        100        110        120 
SLHFDDIDIA FFCAGSEVSK EFIPKATASN CVVIDKSSLF RVDNQVPLIV PEVNLSTLKE 

       130        140        150        160        170        180 
FNTKNIIANP NCIVIPLAVA LKPLDNEIKI KRVVISTYQS VSGAGKAGMD ELYDQTKSKY 

       190        200        210        220        230        240 
VFGENDPKKF PKQIAFNIFP HIGDLNKDGY TSEEAKIASE LNKIIGNHFK ASVTSVRVPV 

       250        260        270        280        290        300 
FIGHSISVNI EFNDKIDAKE VEEILQDADG IVTISNNNYL AYISPVEVVG EDAVYVSRIR 

       310        320        330 
NDVSRDNTIN LWITCDNLRK GAALNSVQIA EELINNYL 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL02968.1.
PIRF97753.
RefSeqNP_360067.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92IJ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272944.RC0430.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL02968; AAL02968; RC0430.
GeneID927572.
KEGGrco:RC0430.
PATRIC17888063. VBIRicCon45613_0487.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0136.
HOGENOMHOG000013357.
KOK00133.
OMAFPIKKFV.
OrthoDBEOG6JB158.
ProtClustDBPRK14874.

Enzyme and pathway databases

UniPathwayUPA00034; UER00016.
UPA00050; UER00463.
UPA00051; UER00464.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_02121. ASADH.
InterProIPR012080. 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]
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.
ProtoNetSearch...

Entry information

Entry nameDHAS_RICCN
AccessionPrimary (citable) accession number: Q92IJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Rickettsia conorii

(strain Malish 7): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways