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Protein

Aspartate-semialdehyde dehydrogenase

Gene

asd

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH.UniRule annotation

Pathway:iL-lysine biosynthesis via DAP pathway

This protein is involved in step 2 of the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. 4-hydroxy-tetrahydrodipicolinate synthase (dapA)
  4. 4-hydroxy-tetrahydrodipicolinate reductase (dapB)
This subpathway is part of the pathway L-lysine biosynthesis via DAP pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate, the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

Pathway:iL-methionine biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes L-homoserine from L-aspartate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homoserine from L-aspartate, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Pathway:iL-threonine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-threonine from L-aspartate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. Bifunctional aspartokinase/homoserine dehydrogenase (thrA)
  4. Homoserine kinase (thrB)
  5. Threonine synthase (thrC)
This subpathway is part of the pathway L-threonine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-threonine from L-aspartate, the pathway L-threonine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei75 – 751NADPUniRule annotation
Binding sitei104 – 1041PhosphateUniRule annotation
Active sitei137 – 1371Acyl-thioester intermediateUniRule annotation
Binding sitei164 – 1641SubstrateUniRule annotation
Binding sitei243 – 2431SubstrateUniRule annotation
Binding sitei246 – 2461PhosphateUniRule annotation
Binding sitei269 – 2691SubstrateUniRule annotation
Active sitei276 – 2761Proton acceptorUniRule annotation
Binding sitei352 – 3521NADPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 144NADPUniRule annotation
Nucleotide bindingi38 – 392NADPUniRule annotation
Nucleotide bindingi167 – 1682NADPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis, Methionine biosynthesis, Threonine biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciBAPH198804:GHMG-456-MONOMER.
UniPathwayiUPA00034; UER00016.
UPA00050; UER00463.
UPA00051; UER00464.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate-semialdehyde dehydrogenaseUniRule annotation (EC:1.2.1.11UniRule annotation)
Short name:
ASA dehydrogenaseUniRule annotation
Short name:
ASADHUniRule annotation
Alternative name(s):
Aspartate-beta-semialdehyde dehydrogenaseUniRule annotation
Gene namesi
Name:asdUniRule annotation
Ordered Locus Names:BUsg_433
OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Taxonomic identifieri198804 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000416 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 371371Aspartate-semialdehyde dehydrogenasePRO_0000141364Add
BLAST

Proteomic databases

PRIDEiQ8K9B5.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi198804.BUsg433.

Structurei

3D structure databases

ProteinModelPortaliQ8K9B5.
SMRiQ8K9B5. Positions 3-368.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aspartate-semialdehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0136.
KOiK00133.
OMAiSCQGGDY.
OrthoDBiEOG67X1PS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_02121. ASADH.
InterProiIPR000319. 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]
PfamiPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
PIRSFiPIRSF000148. ASA_dh. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01745. asd_gamma. 1 hit.
PROSITEiPS01103. ASD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K9B5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKSVGIIGW RGMVGSVLLK RMQEENDFSK IIPYFFSTSQ SGQDGPIINN
60 70 80 90 100
ILSKNLKDAY NINLLQEMDI IITCQGSSYT EKIYPKLRNN NWQGYWIDAA
110 120 130 140 150
STLRMEKDAT IILDPVNLNV INNALDKGIK TFVGGNCTVS LMLMALGGLF
160 170 180 190 200
VNNLIDWVFV STYQAASGAG SRYVIELLKQ MGSLYNVVSK DLLDKSYSVL
210 220 230 240 250
DIEKKVTQES RSKNFPLENF SVPLATSLIP WIDVEMKNGQ SREEWKGQAE
260 270 280 290 300
TNKILNLKKK VLIDGTCVRI SSIRCHSQSF LIKLNKDISL ENIKKIIVNH
310 320 330 340 350
NQWVDVIPNN MQKTLCNLTP SAVTDTLNIP IGRLRKLNID DRYLSAFTVG
360 370
DQLLWGAAEP LRRMLNLLVN I
Length:371
Mass (Da):41,785
Last modified:October 1, 2002 - v1
Checksum:i079A0E1BEAE68318
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013218 Genomic DNA. Translation: AAM67976.1.
RefSeqiWP_011053943.1. NC_004061.1.

Genome annotation databases

EnsemblBacteriaiAAM67976; AAM67976; BUsg_433.
KEGGibas:BUsg433.
PATRICi21247716. VBIBucAph100086_0458.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013218 Genomic DNA. Translation: AAM67976.1.
RefSeqiWP_011053943.1. NC_004061.1.

3D structure databases

ProteinModelPortaliQ8K9B5.
SMRiQ8K9B5. Positions 3-368.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198804.BUsg433.

Proteomic databases

PRIDEiQ8K9B5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM67976; AAM67976; BUsg_433.
KEGGibas:BUsg433.
PATRICi21247716. VBIBucAph100086_0458.

Phylogenomic databases

eggNOGiCOG0136.
KOiK00133.
OMAiSCQGGDY.
OrthoDBiEOG67X1PS.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00016.
UPA00050; UER00463.
UPA00051; UER00464.
BioCyciBAPH198804:GHMG-456-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_02121. ASADH.
InterProiIPR000319. 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]
PfamiPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
PIRSFiPIRSF000148. ASA_dh. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01745. asd_gamma. 1 hit.
PROSITEiPS01103. ASD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sg.

Entry informationi

Entry nameiDHAS_BUCAP
AccessioniPrimary (citable) accession number: Q8K9B5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: July 22, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Buchnera aphidicola (subsp. Schizaphis graminum)
    Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.