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P0A9R0 (DHAS_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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
Ordered Locus Names:Z4797, ECs4278
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length367 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 – 367367Aspartate-semialdehyde dehydrogenase HAMAP MF_02121
PRO_0000141370

Regions

Nucleotide binding10 – 134NADP By similarity
Nucleotide binding37 – 382NADP By similarity
Nucleotide binding165 – 1662NADP By similarity

Sites

Active site1351Acyl-thioester intermediate By similarity
Active site2741Proton acceptor By similarity
Binding site731NADP By similarity
Binding site1021Phosphate By similarity
Binding site1621Substrate By similarity
Binding site1931NADP; via carbonyl oxygen By similarity
Binding site2411Substrate By similarity
Binding site2441Phosphate By similarity
Binding site2671Substrate By similarity
Binding site3501NADP By similarity

Amino acid modifications

Modified residue1351S-cysteinyl cysteine; in inhibited form By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A9R0 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: F53D4C36EA7CC201

FASTA36740,018
        10         20         30         40         50         60 
MKNVGFIGWR GMVGSVLMQR MVEERDFDAI RPVFFSTSQL GQAAPSFGGT TGTLQDAFDL 

        70         80         90        100        110        120 
EALKALDIIV TCQGGDYTNE IYPKLRESGW QGYWIDAASS LRMKDDAIII LDPVNQDVIT 

       130        140        150        160        170        180 
DGLNNGIRTF VGGNCTVSLM LMSLGGLFAN DLVDWVSVAT YQAASGGGAR HMRELLTQMG 

       190        200        210        220        230        240 
HLYGHVADEL ATPSSAILDI ERKVTTLTRS GELPVDNFGV PLAGSLIPWI DKQLDNGQSR 

       250        260        270        280        290        300 
EEWKGQAETN KILNTSSVIP VDGLCVRVGA LRCHSQAFTI KLKKDVSIPT VEELLAAHNP 

       310        320        330        340        350        360 
WAKVVPNDRE ITMRELTPAA VTGTLTTPVG RLRKLNMGPE FLSAFTVGDQ LLWGAAEPLR 


RMLRQLA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005174 Genomic DNA. Translation: AAG58539.1.
BA000007 Genomic DNA. Translation: BAB37701.1.
PIRF91163.
G86009.
RefSeqNP_289978.1. NC_002655.2.
NP_312305.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0A9R0.
SMRP0A9R0. Positions 1-367.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000024507; EBESCP00000023400; EBESCG00000023561.
EBESCT00000057828; EBESCP00000055656; EBESCG00000056876.
GeneID915867.
958911.
GenomeReviewsGene locus Z4797 in contig AE005174_GR.
Gene locus ECs4278 in contig BA000007_GR.
KEGGece:Z4797.
ecs:ECs4278.
PATRIC18358121. VBIEscCol44059_4227.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000010426.
HOGENOMHBG289760.
OMAIDGLCVR.
ProtClustDBPRK06598.

Enzyme and pathway databases

BioCycECOL83334:ECS4278-MONOMER.

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_ECO57
AccessionPrimary (citable) accession number: P0A9R0
Secondary accession number(s): P00353
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 25, 2012
This is version 52 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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