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P41394 (DHAS_LEPIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 102. 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

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:LB_355
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) [Reference proteome] [HAMAP]
Taxonomic identifier189518 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length349 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 – 349349Aspartate-semialdehyde dehydrogenase HAMAP-Rule MF_02121
PRO_0000141380

Regions

Nucleotide binding12 – 154NADP By similarity
Nucleotide binding39 – 402NADP By similarity
Nucleotide binding178 – 1792NADP By similarity
Nucleotide binding326 – 3272NADP By similarity

Sites

Active site1481Acyl-thioester intermediate By similarity
Active site2411Proton acceptor By similarity
Binding site1131Phosphate By similarity
Binding site1751Substrate By similarity
Binding site2011Substrate By similarity
Binding site2041Phosphate By similarity
Binding site2341Substrate By similarity

Experimental info

Sequence conflict311V → I in AAB21985. Ref.1
Sequence conflict311V → I in AAA25262. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P41394 [UniParc].

Last modified December 6, 2002. Version 2.
Checksum: 1DB092D05CE66254

FASTA34938,018
        10         20         30         40         50         60 
MSRVKVAVLG ATGSVGQRFI QLLDHHPFFE VTHLCASENS AGKTYGEVMK TRWKISSDIP 

        70         80         90        100        110        120 
AYAKNLVITT PDPAKTKDVV LAFSGLDSNV AGEVEKNYAN AGIHIISNSK NHRMDPTVPI 

       130        140        150        160        170        180 
LSAEVNSSHL EVLTSQKTKG KIITNSNCTI MGVTISLKPL LDRFGIESVM LFSMQAISGA 

       190        200        210        220        230        240 
GYPGVPTMDI LGNVIPHIGG EEEKAEIEPL KCLGKVENGK ILHADFSISA HCNRVPVFDG 

       250        260        270        280        290        300 
HTVCVSVKFK KKPSREEIIS SWKDFSGEPQ TLGLPLAPNP VILFREEEDR PQPRLDLDTG 

       310        320        330        340 
KGMTTVIGRL RPDPILDWKY VVLSHNTIRG AAGAALLNAE LLYKKKFLG 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of dapD, aroD and asd of Leptospira interrogans serovar icterohaemorrhagiae, and nucleotide sequence of the asd gene."
Baril C., Richaud C., Fourni E., Baranton G., Saint-Girons I.
J. Gen. Microbiol. 138:47-53(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Serogroup Icterohaemorrhagiae.
[2]"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing."
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. expand/collapse author list , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.
Nature 422:888-893(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 56601.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S92223 Genomic DNA. Translation: AAB21985.1.
M77500 Genomic DNA. Translation: AAA25262.1.
AE010301 Genomic DNA. Translation: AAN51914.1.
PIRA44846.
RefSeqNP_714899.1. NC_004343.2.

3D structure databases

ProteinModelPortalP41394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING189518.LB355.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN51914; AAN51914; LB_355.
GeneID1153914.
KEGGlil:LB_355.
PATRIC22390238. VBILepInt91350_4670.

Phylogenomic databases

eggNOGCOG0136.
HOGENOMHOG000013358.
KOK00133.
OMAMSIVVGR.
OrthoDBEOG6JB158.

Enzyme and pathway databases

BioCycLINT189518:GJBB-3740-MONOMER.
UniPathwayUPA00034; UER00016.
UPA00050; UER00463.
UPA00051; UER00464.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_02121. ASADH.
InterProIPR000319. Asp-semialdehyde_DH_CS.
IPR005676. Asp_semi-ald_DH_pep-lack.
IPR012080. Asp_semialdehyde_DH.
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]
TIGRFAMsTIGR00978. asd_EA. 1 hit.
PROSITEPS01103. ASD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHAS_LEPIN
AccessionPrimary (citable) accession number: P41394
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 6, 2002
Last modified: May 14, 2014
This is version 102 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways