Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aspartate-semialdehyde dehydrogenase

Gene

asd

Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Status
Unreviewed-Annotation score: -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

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.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)DescriptionActionsGraphical viewLength
Binding sitei71NADPCombined sources1
Binding sitei94NADPCombined sources1
Binding sitei99PhosphateUniRule annotation1
Active sitei128Acyl-thioester intermediateUniRule annotation1
Binding sitei155SubstrateUniRule annotation1
Binding sitei245SubstrateUniRule annotation1
Active sitei252Proton acceptorUniRule annotation1
Binding sitei325NADPUniRule annotation1
Binding sitei329NADP; via carbonyl oxygenCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi9 – 14NADPCombined sources6
Nucleotide bindingi11 – 14NADPUniRule annotation4
Nucleotide bindingi36 – 40NADPCombined sources5
Nucleotide bindingi39 – 40NADPUniRule annotation2
Nucleotide bindingi126 – 128NADPCombined sources3
Nucleotide bindingi158 – 159NADPUniRule annotation2
Nucleotide bindingi162 – 163NADPCombined sources2

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductaseUniRule annotationImported
Biological processAmino-acid biosynthesis, Diaminopimelate biosynthesisUniRule annotation, Lysine biosynthesisUniRule annotation, Methionine biosynthesisUniRule annotation, Threonine biosynthesisUniRule annotation
LigandNADPUniRule annotationCombined sources, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciSPNE171101:SPR0918-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

Interactioni

Subunit structurei

Homodimer.UniRule annotation

GO - Molecular functioni

Protein-protein interaction databases

STRINGi171101.spr0918

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 119Semialdhyde_dhInterPro annotationAdd BLAST116

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CM3 Bacteria
COG0136 LUCA
HOGENOMiHOG000013357
KOiK00133
OMAiCEEEMKM

Family and domain databases

HAMAPiMF_02121 ASADH, 1 hit
InterProiView protein in InterPro
IPR012080 Asp_semialdehyde_DH
IPR005986 Asp_semialdehyde_DH_beta
IPR036291 NAD(P)-bd_dom_sf
IPR000534 Semialdehyde_DH_NAD-bd
IPR012280 Semialdhyde_DH_dimer_dom
PfamiView protein in Pfam
PF01118 Semialdhyde_dh, 1 hit
PF02774 Semialdhyde_dhC, 1 hit
SMARTiView protein in SMART
SM00859 Semialdhyde_dh, 1 hit
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
PATRICifig|171101.6.peg.1005

Similar proteinsi

Entry informationi

Entry nameiQ8DQ00_STRR6
AccessioniPrimary (citable) accession number: Q8DQ00
Entry historyiIntegrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: June 20, 2018
This is version 107 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health