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P44801 (DHAS_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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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:HI_0646
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length371 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. Ref.2

Catalytic activity

L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH. Ref.2 Ref.4

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. Ref.3

Domain

Consists of two domains, an N-terminal nucleotide-binding domain and a C-terminal dimerization domain. Ref.3

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.24 mM for L-aspartate 4-semialdehyde Ref.2 Ref.4

KM=0.15 mM for NADP+

KM=1.6 mM for phosphate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 371371Aspartate-semialdehyde dehydrogenase HAMAP MF_02121
PRO_0000141375

Regions

Nucleotide binding10 – 134NADP HAMAP MF_02121
Nucleotide binding37 – 382NADP HAMAP MF_02121

Sites

Active site1361Acyl-thioester intermediate
Active site2771Proton acceptor
Binding site741NADP
Binding site1031Phosphate
Binding site1631Substrate
Binding site1661NADP; via carbonyl oxygen
Binding site2431Substrate
Binding site2461Phosphate
Binding site2701Substrate
Binding site3531NADP

Experimental info

Mutagenesis1031R → K: 2-fold increase in affinity for ASA, 23-fold decrease in affinity for phosphate, and 275-fold decrease in activity. Ref.4
Mutagenesis1031R → L: 7-fold increase in affinity for ASA, 150-fold decrease in affinity for phosphate, and 1400-fold decrease in activity. Ref.4
Mutagenesis2431E → D: No change in affinity for ASA and 82-fold decrease in activity. Ref.4
Mutagenesis2461K → R: 2-fold increase in affinity for ASA, nearly no change in affinity for phosphate, and 30-fold decrease in activity. Ref.4
Mutagenesis2701R → K: 2-fold decrease in affinity for ASA and 825-fold decrease in activity. Ref.4

Secondary structure

1 ............................................................. 371
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P44801 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: E44CE5B90F2AF041

FASTA37140,539
        10         20         30         40         50         60 
MKNVGFIGWR GMVGSVLMDR MSQENDFENL NPVFFTTSQA GQKAPVFGGK DAGDLKSAFD 

        70         80         90        100        110        120 
IEELKKLDII VTCQGGDYTN EVYPKLKATG WDGYWVDAAS ALRMKDDAII VLDPVNQHVI 

       130        140        150        160        170        180 
SEGLKKGIKT FVGGNCTVSL MLMAIGGLFE KDLVEWISVA TYQAASGAGA KNMRELLSQM 

       190        200        210        220        230        240 
GLLEQAVSSE LKDPASSILD IERKVTAKMR ADNFPTDNFG AALGGSLIPW IDKLLPETGQ 

       250        260        270        280        290        300 
TKEEWKGYAE TNKILGLSDN PIPVDGLCVR IGALRCHSQA FTIKLKKDLP LEEIEQIIAS 

       310        320        330        340        350        360 
HNEWVKVIPN DKEITLRELT PAKVTGTLSV PVGRLRKLAM GPEYLAAFTV GDQLLWGAAE 

       370 
PVRRILKQLV A

« Hide

References

« Hide 'large scale' references
[1]"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. expand/collapse author list , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.
Science 269:496-512(1995) [PubMed: 7542800] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]"Expression and purification of aspartate beta-semialdehyde dehydrogenase from infectious microorganisms."
Moore R.A., Bocik W.E., Viola R.E.
Protein Expr. Purif. 25:189-194(2002) [PubMed: 12071715] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS.
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[3]"Capture of an intermediate in the catalytic cycle of L-aspartate-beta-semialdehyde dehydrogenase."
Blanco J., Moore R.A., Viola R.E.
Proc. Natl. Acad. Sci. U.S.A. 100:12613-12617(2003) [PubMed: 14559965] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH L-ASPARTATE-SEMIALDEHYDE AND PHOSPHATE, SUBUNIT, DOMAIN, CATALYTIC MECHANISM.
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[4]"The role of substrate-binding groups in the mechanism of aspartate-beta-semialdehyde dehydrogenase."
Blanco J., Moore R.A., Faehnle C.R., Coe D.M., Viola R.E.
Acta Crystallogr. D 60:1388-1395(2004) [PubMed: 15272161] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF MUTANTS LEU-103; LYS-103; SER-136; ASP-243; ARG-246; LYS-270 AND ASN-277 IN COMPLEX WITH NADP, CATALYTIC ACTIVITY, KINETIC STUDIES, MUTAGENESIS OF ARG-103; GLU-243; LYS-246 AND ARG-270.
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[5]"Structural basis for discrimination between oxyanion substrates or inhibitors in aspartate-beta-semialdehyde dehydrogenase."
Faehnle C.R., Blanco J., Viola R.E.
Acta Crystallogr. D 60:2320-2324(2004) [PubMed: 15583380] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEXES WITH ARSENATE AND PERIODATE IONS.
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42023 Genomic DNA. Translation: AAC22306.1.
PIRB64084.
RefSeqNP_438806.1. NC_000907.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NWCX-ray2.04A/B1-371[»]
1NWHX-ray2.00A/B1-371[»]
1NX6X-ray2.15A1-371[»]
1OZAX-ray2.06A1-371[»]
1PQPX-ray2.06A1-371[»]
1PQUX-ray1.92A/B/C/D1-371[»]
1PR3X-ray2.15A1-371[»]
1PS8X-ray2.40A1-371[»]
1PU2X-ray2.06A1-371[»]
1Q2XX-ray2.05A/B1-371[»]
1TA4X-ray2.28A1-371[»]
1TB4X-ray2.15A1-371[»]
ProteinModelPortalP44801.
SMRP44801. Positions 1-371.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID949960.
GenomeReviewsGene locus HI_0646 in contig L42023_GR.
KEGGhin:HI0646.
NMPDRfig|71421.1.peg.616.
PATRIC20189907. VBIHaeInf48452_0675.
TIGRHI_0646.

Phylogenomic databases

HOGENOMHBG289760.
OMAIDGLCVR.
ProtClustDBPRK06598.

Enzyme and pathway databases

BioCycHINF71421:HI_0646-MONOMER.
BRENDA1.2.1.11. 2529.

Family and domain databases

HAMAPMF_02121. ASADH.
[Tree]
InterProIPR000319. Asp-semialdehyde_DH_CS.
IPR011534. Asp_ADH_gamma-type.
IPR012080. Asp_semialdehyde_DH.
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]
TIGRFAMsTIGR01745. Asd_gamma. 1 hit.
PROSITEPS01103. ASD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHAS_HAEIN
AccessionPrimary (citable) accession number: P44801
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 25, 2012
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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