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Protein

Aspartate-semialdehyde dehydrogenase

Gene

asd

Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

Pathwayi: L-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. Aspartokinase (lysC)
  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.

Pathwayi: L-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. Aspartokinase (lysC)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. Homoserine dehydrogenase (hom)
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.

Pathwayi: L-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. Aspartokinase (lysC)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. Homoserine dehydrogenase (hom)
  4. Homoserine kinase (thrB)
  5. no protein annotated in this organism
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 sitei71 – 711NADPCombined sources
Binding sitei94 – 941NADPCombined sources
Binding sitei99 – 991PhosphateUniRule annotation
Active sitei128 – 1281Acyl-thioester intermediateUniRule annotation
Binding sitei155 – 1551SubstrateUniRule annotation
Binding sitei245 – 2451SubstrateUniRule annotation
Active sitei252 – 2521Proton acceptorUniRule annotation
Binding sitei325 – 3251NADPUniRule annotation
Binding sitei329 – 3291NADP; via carbonyl oxygenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 146NADPCombined sources
Nucleotide bindingi11 – 144NADPUniRule annotation
Nucleotide bindingi36 – 405NADPCombined sources
Nucleotide bindingi39 – 402NADPUniRule annotation
Nucleotide bindingi126 – 1283NADPCombined sources
Nucleotide bindingi158 – 1592NADPUniRule annotation
Nucleotide bindingi162 – 1632NADPCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationImported

Keywords - Biological processi

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

Keywords - Ligandi

NADPUniRule annotationCombined sources, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciSPNE171101:GJC8-930-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 annotationImported
Ordered Locus Names:spr0918Imported
OrganismiStreptococcus pneumoniae (strain ATCC BAA-255 / R6)Imported
Taxonomic identifieri171101 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000586 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi171101.spr0918.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q1LX-ray2.30A/B/C/D1-358[»]
4R3NX-ray1.35A/B1-358[»]
ProteinModelPortaliQ8DQ00.
SMRiQ8DQ00. Positions 2-358.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 119116Semialdhyde_dhInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the aspartate-semialdehyde dehydrogenase family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiENOG4105CM3. Bacteria.
COG0136. LUCA.
HOGENOMiHOG000013357.
KOiK00133.
OMAiKWHKGII.
OrthoDBiEOG6JB158.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_02121. ASADH.
InterProiIPR012080. 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]
PfamiPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
PIRSFiPIRSF000148. ASA_dh. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01296. asd_B. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8DQ00-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGYTVAVVGA TGAVGAQMIK MLEESTLPID KIRYLASARS AGKSLKFKDQ
60 70 80 90 100
DITIEETTET AFEGVDIALF SAGSSTSAKY APYAVKAGVV VVDNTSYFRQ
110 120 130 140 150
NPDVPLVVPE VNAHALDAHN GIIACPNCST IQMMVALEPV RQKWGLDRII
160 170 180 190 200
VSTYQAVSGA GMGAILETQR ELREVLNDGV KPCDLHAEIL PSGGDKKHYP
210 220 230 240 250
IAFNALPQID VFTDNDYTYE EMKMTKETKK IMEDDSIAVS ATCVRIPVLS
260 270 280 290 300
AHSESVYIET KEVAPIEEVK AAIAAFPGAV LEDDVAHQIY PQAINAVGSR
310 320 330 340 350
DTFVGRIRKD LDAEKGIHMW VVSDNLLKGA AWNSVQIAET LHERGLVRPT

AELKFELK
Length:358
Mass (Da):38,924
Last modified:March 1, 2003 - v1
Checksum:i366715956847C96C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE007317 Genomic DNA. Translation: AAK99722.1.
PIRiF97986.
RefSeqiNP_358512.1. NC_003098.1.
WP_000542475.1. NC_003098.1.

Genome annotation databases

EnsemblBacteriaiAAK99722; AAK99722; spr0918.
GeneIDi933797.
KEGGispr:spr0918.
PATRICi19701775. VBIStrPne107296_1005.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE007317 Genomic DNA. Translation: AAK99722.1.
PIRiF97986.
RefSeqiNP_358512.1. NC_003098.1.
WP_000542475.1. NC_003098.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q1LX-ray2.30A/B/C/D1-358[»]
4R3NX-ray1.35A/B1-358[»]
ProteinModelPortaliQ8DQ00.
SMRiQ8DQ00. Positions 2-358.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi171101.spr0918.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK99722; AAK99722; spr0918.
GeneIDi933797.
KEGGispr:spr0918.
PATRICi19701775. VBIStrPne107296_1005.

Phylogenomic databases

eggNOGiENOG4105CM3. Bacteria.
COG0136. LUCA.
HOGENOMiHOG000013357.
KOiK00133.
OMAiKWHKGII.
OrthoDBiEOG6JB158.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00016.
UPA00050; UER00463.
UPA00051; UER00464.
BioCyciSPNE171101:GJC8-930-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_02121. ASADH.
InterProiIPR012080. 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]
PfamiPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
PIRSFiPIRSF000148. ASA_dh. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01296. asd_B. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-255 / R6Imported.
  2. "Structural characterization of inhibitors with selectivity against members of a homologous enzyme family."
    Pavlovsky A.G., Liu X., Faehnle C.R., Potente N., Viola R.E.
    Chem. Biol. Drug Des. 79:128-136(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS).
  3. "A cautionary tale of structure-guided inhibitor development against an essential enzyme in the aspartate-biosynthetic pathway."
    Pavlovsky A.G., Thangavelu B., Bhansali P., Viola R.E.
    Acta Crystallogr. D 70:3244-3252(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH NADP.

Entry informationi

Entry nameiQ8DQ00_STRR6
AccessioniPrimary (citable) accession number: Q8DQ00
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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 one 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.