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Protein

Aspartate-semialdehyde dehydrogenase

Gene

asd

Organism
Acidiphilium cryptum (strain JF-5)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001PhosphateUniRule annotation
Active sitei135 – 1351Acyl-thioester intermediateUniRule annotation
Binding sitei162 – 1621SubstrateUniRule annotation
Binding sitei216 – 2161SubstrateUniRule annotation
Binding sitei219 – 2191PhosphateUniRule annotation
Binding sitei240 – 2401SubstrateUniRule annotation
Active sitei247 – 2471Proton acceptorUniRule annotation
Binding sitei320 – 3201NADPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 144NADPUniRule annotation
Nucleotide bindingi39 – 402NADPUniRule annotation
Nucleotide bindingi165 – 1662NADPUniRule annotation

GO - Molecular functioni

  1. aspartate-semialdehyde dehydrogenase activity Source: UniProtKB-HAMAP
  2. N-acetyl-gamma-glutamyl-phosphate reductase activity Source: InterPro
  3. NAD binding Source: InterPro
  4. NADP binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' L-methionine biosynthetic process Source: UniProtKB-HAMAP
  2. diaminopimelate biosynthetic process Source: UniProtKB-HAMAP
  3. isoleucine biosynthetic process Source: InterPro
  4. lysine biosynthetic process via diaminopimelate Source: UniProtKB-HAMAP
  5. threonine biosynthetic process Source: UniProtKB-HAMAP
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

BioCyciACRY349163:GHET-1743-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:Acry_1717Imported
OrganismiAcidiphilium cryptum (strain JF-5)Imported
Taxonomic identifieri349163 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium
ProteomesiUP000000245 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi349163.Acry_1717.

Structurei

3D structure databases

ProteinModelPortaliA5FZ89.
SMRiA5FZ89. Positions 2-339.
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.

A5FZ89-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYKVAVVGA TGAVGREMLK TLAERNFPAS EVIALASPRS AGQQVSFGDE
60 70 80 90 100
AILTVKNLET FDFRGVDFGL FSPGASISAV HAPRAAEAGC IVIDNTSHFR
110 120 130 140 150
MEPDVPLVVP EVNTHALEAF MAKPDWRRII ANPNCSTIQM VVALKPLHEK
160 170 180 190 200
FGIRRVSVAT YQSVSGAGKE GMDELERATK ATYVHETTKP EVFTKPIAFN
210 220 230 240 250
VIPHIDVFMK DGATKEEWKM TVETRKILDP DIAVFATCVR VPVFIGHGEA
260 270 280 290 300
VHVEFANPAP LEAARAALRA APGVTLFDER EDGGYVTPLE CQGEDAVYVS
310 320 330 340
RLRVDPTVPH GLGFWCVSDN LRKGAALNAV QIAETIVKRG LIGKKAA
Length:347
Mass (Da):37,519
Last modified:June 12, 2007 - v1
Checksum:iF85F82E6690F6117
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000697 Genomic DNA. Translation: ABQ30921.1.
RefSeqiYP_001234840.1. NC_009484.1.

Genome annotation databases

EnsemblBacteriaiABQ30921; ABQ30921; Acry_1717.
KEGGiacr:Acry_1717.
PATRICi20648472. VBIAciCry6074_2217.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000697 Genomic DNA. Translation: ABQ30921.1.
RefSeqiYP_001234840.1. NC_009484.1.

3D structure databases

ProteinModelPortaliA5FZ89.
SMRiA5FZ89. Positions 2-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi349163.Acry_1717.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ30921; ABQ30921; Acry_1717.
KEGGiacr:Acry_1717.
PATRICi20648472. VBIAciCry6074_2217.

Phylogenomic databases

eggNOGiCOG0136.
HOGENOMiHOG000013357.
KOiK00133.
OMAiWRMDPTK.
OrthoDBiEOG6JB158.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00016.
UPA00050; UER00463.
UPA00051; UER00464.
BioCyciACRY349163:GHET-1743-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: JF-5Imported.

Entry informationi

Entry nameiA5FZ89_ACICJ
AccessioniPrimary (citable) accession number: A5FZ89
Entry historyi
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: April 29, 2015
This is version 57 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.