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
Desulfotomaculum reducens (strain MI-1)
Status
Unreviewed-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: 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 (Dred_1940), Aspartokinase (Dred_1167)
  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: 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 (Dred_1940), Aspartokinase (Dred_1167)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. Homoserine dehydrogenase (Dred_1165)
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: 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 (Dred_1940), Aspartokinase (Dred_1167)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. Homoserine dehydrogenase (Dred_1165)
  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 sitei99 – 991PhosphateUniRule annotation
Active sitei128 – 1281Acyl-thioester intermediateUniRule annotation
Binding sitei155 – 1551SubstrateUniRule annotation
Binding sitei234 – 2341SubstrateUniRule annotation
Active sitei241 – 2411Proton acceptorUniRule annotation
Binding sitei314 – 3141NADPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 154NADPUniRule annotation
Nucleotide bindingi40 – 412NADPUniRule annotation
Nucleotide bindingi158 – 1592NADPUniRule annotation

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 annotation

Enzyme and pathway databases

BioCyciDRED349161:GHP6-1996-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:Dred_1941Imported
OrganismiDesulfotomaculum reducens (strain MI-1)Imported
Taxonomic identifieri349161 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfotomaculum
ProteomesiUP000001556 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi349161.Dred_1941.

Structurei

3D structure databases

ProteinModelPortaliA4J5V7.
SMRiA4J5V7. Positions 5-331.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aspartate-semialdehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0136.
HOGENOMiHOG000013357.
KOiK00133.
OMAiWRMDPTK.
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]
TIGRFAMsiTIGR01296. asd_B. 1 hit.

Sequencei

Sequence statusi: Complete.

A4J5V7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTVNLVIVG ATGAVGKEIL NILKERNFPI NKLRLCATSR SAGTEIEFQG
60 70 80 90 100
HKYLVEETTP DSFNGMDVAL FAGGKASLEF GKAAVERGCV VIDNSSNYRM
110 120 130 140 150
DPEVPLVVPE VNPEDVKKHK GIIANPNCST IIMVVALKPL HDAAGIKRVV
160 170 180 190 200
VSTYQAVSGA GKEGIEELTE QVKATLDGRE YPPNKFAHQI AFNLIPHIDV
210 220 230 240 250
FQEMDYTKEE WKMVKETQKI MHDDNIKITA TTVRVPIYRS HSESINIETE
260 270 280 290 300
EKITADQARE ILANAPGIIV QDDVTNKVYP MPLFTSDRDE VFVGRIREDN
310 320 330 340
TIDKGLNLWV VGDQIRKGAA TNAVQIAELV LKYDSLMKKE
Length:340
Mass (Da):37,691
Last modified:May 1, 2007 - v1
Checksum:iC54DCB13E948F775
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000612 Genomic DNA. Translation: ABO50460.1.
RefSeqiWP_011878270.1. NC_009253.1.
YP_001113285.1. NC_009253.1.

Genome annotation databases

EnsemblBacteriaiABO50460; ABO50460; Dred_1941.
KEGGidrm:Dred_1941.
PATRICi21730117. VBIDesRed82656_2131.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000612 Genomic DNA. Translation: ABO50460.1.
RefSeqiWP_011878270.1. NC_009253.1.
YP_001113285.1. NC_009253.1.

3D structure databases

ProteinModelPortaliA4J5V7.
SMRiA4J5V7. Positions 5-331.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi349161.Dred_1941.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABO50460; ABO50460; Dred_1941.
KEGGidrm:Dred_1941.
PATRICi21730117. VBIDesRed82656_2131.

Phylogenomic databases

eggNOGiCOG0136.
HOGENOMiHOG000013357.
KOiK00133.
OMAiWRMDPTK.
OrthoDBiEOG6JB158.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00016.
UPA00050; UER00463.
UPA00051; UER00464.
BioCyciDRED349161:GHP6-1996-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]
TIGRFAMsiTIGR01296. asd_B. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MI-1Imported.

Entry informationi

Entry nameiA4J5V7_DESRM
AccessioniPrimary (citable) accession number: A4J5V7
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2007
Last sequence update: May 1, 2007
Last modified: April 1, 2015
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.