SubmitCancel

Skip Header

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

A5FZ89

- A5FZ89_ACICJ

UniProt

A5FZ89 - A5FZ89_ACICJ

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Aspartate-semialdehyde dehydrogenase
Gene
asd, Acry_1717
Organism
Acidiphilium cryptum (strain JF-5)
Status
Unreviewed - 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 By similarity.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 – 1001Phosphate By similarityUniRule annotation
Active sitei135 – 1351Acyl-thioester intermediate By similarityUniRule annotation
Binding sitei162 – 1621Substrate By similarityUniRule annotation
Binding sitei216 – 2161Substrate By similarityUniRule annotation
Binding sitei219 – 2191Phosphate By similarityUniRule annotation
Binding sitei240 – 2401Substrate By similarityUniRule annotation
Active sitei247 – 2471Proton acceptor By similarityUniRule annotation
Binding sitei320 – 3201NADP By similarityUniRule annotation

Regions

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

GO - Molecular functioni

  1. N-acetyl-gamma-glutamyl-phosphate reductase activity Source: InterPro
  2. NAD binding Source: InterPro
  3. NADP binding Source: UniProtKB-HAMAP
  4. aspartate-semialdehyde dehydrogenase activity 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 dehydrogenase
Gene namesi
Name:asdUniRule annotation
Ordered Locus Names:Acry_1717Imported
OrganismiAcidiphilium cryptum (strain JF-5)Imported
Taxonomic identifieri349163 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium
ProteomesiUP000000245: Chromosome

Subcellular locationi

GO - Cellular componenti

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

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi349163.Acry_1717.

Structurei

3D structure databases

ProteinModelPortaliA5FZ89.
SMRiA5FZ89. Positions 2-339.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0136.
HOGENOMiHOG000013357.
KOiK00133.
OMAiNDPKKFP.
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

MAYKVAVVGA TGAVGREMLK TLAERNFPAS EVIALASPRS AGQQVSFGDE    50
AILTVKNLET FDFRGVDFGL FSPGASISAV HAPRAAEAGC IVIDNTSHFR 100
MEPDVPLVVP EVNTHALEAF MAKPDWRRII ANPNCSTIQM VVALKPLHEK 150
FGIRRVSVAT YQSVSGAGKE GMDELERATK ATYVHETTKP EVFTKPIAFN 200
VIPHIDVFMK DGATKEEWKM TVETRKILDP DIAVFATCVR VPVFIGHGEA 250
VHVEFANPAP LEAARAALRA APGVTLFDER EDGGYVTPLE CQGEDAVYVS 300
RLRVDPTVPH GLGFWCVSDN LRKGAALNAV QIAETIVKRG LIGKKAA 347
Length:347
Mass (Da):37,519
Last modified:June 12, 2007 - v1
Checksum:iF85F82E6690F6117
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000697 Genomic DNA. Translation: ABQ30921.1.
RefSeqiYP_001234840.1. NC_009484.1.

Genome annotation databases

EnsemblBacteriaiABQ30921; ABQ30921; Acry_1717.
GeneIDi5161283.
KEGGiacr:Acry_1717.
PATRICi20648472. VBIAciCry6074_2217.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000697 Genomic DNA. Translation: ABQ30921.1 .
RefSeqi YP_001234840.1. NC_009484.1.

3D structure databases

ProteinModelPortali A5FZ89.
SMRi A5FZ89. Positions 2-339.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349163.Acry_1717.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ30921 ; ABQ30921 ; Acry_1717 .
GeneIDi 5161283.
KEGGi acr:Acry_1717.
PATRICi 20648472. VBIAciCry6074_2217.

Phylogenomic databases

eggNOGi COG0136.
HOGENOMi HOG000013357.
KOi K00133.
OMAi NDPKKFP.
OrthoDBi EOG6JB158.

Enzyme and pathway databases

UniPathwayi UPA00034 ; UER00016 .
UPA00050 ; UER00463 .
UPA00051 ; UER00464 .
BioCyci ACRY349163:GHET-1743-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_02121. ASADH.
InterProi IPR012080. 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 ]
Pfami PF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view ]
PIRSFi PIRSF000148. ASA_dh. 1 hit.
SMARTi SM00859. Semialdhyde_dh. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01296. asd_B. 1 hit.
ProtoNeti Search...

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: June 11, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi