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A4J5V7

- A4J5V7_DESRM

UniProt

A4J5V7 - A4J5V7_DESRM

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Protein

Aspartate-semialdehyde dehydrogenase

Gene

asd

Organism
Desulfotomaculum reducens (strain MI-1)
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.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 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

  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

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: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
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.
OMAiANKGCIV.
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.
RefSeqiYP_001113285.1. NC_009253.1.

Genome annotation databases

EnsemblBacteriaiABO50460; ABO50460; Dred_1941.
GeneIDi4956285.
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 .
RefSeqi YP_001113285.1. NC_009253.1.

3D structure databases

ProteinModelPortali A4J5V7.
SMRi A4J5V7. Positions 5-331.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349161.Dred_1941.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABO50460 ; ABO50460 ; Dred_1941 .
GeneIDi 4956285.
KEGGi drm:Dred_1941.
PATRICi 21730117. VBIDesRed82656_2131.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00034 ; UER00016 .
UPA00050 ; UER00463 .
UPA00051 ; UER00464 .
BioCyci DRED349161:GHP6-1996-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: 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: October 29, 2014
This is version 55 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