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A4J5V7 (A4J5V7_DESRM) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Aspartate-semialdehyde dehydrogenase HAMAP-Rule MF_02121
Short name=ASA dehydrogenase HAMAP-Rule MF_02121
Short name=ASADH HAMAP-Rule MF_02121
EC=1.2.1.11 HAMAP-Rule MF_02121
Alternative name(s):
Aspartate-beta-semialdehyde dehydrogenase HAMAP-Rule MF_02121
Gene names
Name:asd HAMAP-Rule MF_02121
Ordered Locus Names:Dred_1941
OrganismDesulfotomaculum reducens (strain MI-1) [Complete proteome] [HAMAP] EMBL ABO50460.1
Taxonomic identifier349161 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Peptococcaceae › Desulfotomaculum ›

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate By similarity. HAMAP-Rule MF_02121

Catalytic activity

L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH. HAMAP-Rule MF_02121

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. HAMAP-Rule MF_02121

Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. HAMAP-Rule MF_02121

Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. HAMAP-Rule MF_02121

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_02121

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family. RuleBase RU004041 HAMAP-Rule MF_02121

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding12 – 154NADP By similarity HAMAP-Rule MF_02121
Nucleotide binding40 – 412NADP By similarity HAMAP-Rule MF_02121
Nucleotide binding158 – 1592NADP By similarity HAMAP-Rule MF_02121

Sites

Active site1281Acyl-thioester intermediate By similarity HAMAP-Rule MF_02121 PIRSR PIRSR000148-1
Active site2411Proton acceptor By similarity HAMAP-Rule MF_02121 PIRSR PIRSR000148-1
Binding site991Phosphate By similarity HAMAP-Rule MF_02121
Binding site1551Substrate By similarity HAMAP-Rule MF_02121
Binding site2341Substrate By similarity HAMAP-Rule MF_02121
Binding site3141NADP By similarity HAMAP-Rule MF_02121

Sequences

Sequence LengthMass (Da)Tools
A4J5V7 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: C54DCB13E948F775

FASTA34037,691
        10         20         30         40         50         60 
MNTVNLVIVG ATGAVGKEIL NILKERNFPI NKLRLCATSR SAGTEIEFQG HKYLVEETTP 

        70         80         90        100        110        120 
DSFNGMDVAL FAGGKASLEF GKAAVERGCV VIDNSSNYRM DPEVPLVVPE VNPEDVKKHK 

       130        140        150        160        170        180 
GIIANPNCST IIMVVALKPL HDAAGIKRVV VSTYQAVSGA GKEGIEELTE QVKATLDGRE 

       190        200        210        220        230        240 
YPPNKFAHQI AFNLIPHIDV FQEMDYTKEE WKMVKETQKI MHDDNIKITA TTVRVPIYRS 

       250        260        270        280        290        300 
HSESINIETE EKITADQARE ILANAPGIIV QDDVTNKVYP MPLFTSDRDE VFVGRIREDN 

       310        320        330        340 
TIDKGLNLWV VGDQIRKGAA TNAVQIAELV LKYDSLMKKE

« Hide

References

[1]"Complete sequence of Desulfotomaculum reducens MI-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MI-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000612 Genomic DNA. Translation: ABO50460.1.
RefSeqYP_001113285.1. NC_009253.1.

3D structure databases

ProteinModelPortalA4J5V7.
SMRA4J5V7. Positions 5-331.
ModBaseSearch...

Protein-protein interaction databases

STRING349161.Dred_1941.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO50460; ABO50460; Dred_1941.
GeneID4956285.
KEGGdrm:Dred_1941.
PATRIC21730117. VBIDesRed82656_2131.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0136.
HOGENOMHOG000013357.
KOK00133.
OMAPYPLAFN.

Enzyme and pathway databases

BioCycDRED349161:GHP6-2038-MONOMER.
UniPathwayUPA00034; UER00016.
UPA00050; UER00463.
UPA00051; UER00464.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_02121. ASADH.
InterProIPR012080. 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]
PfamPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
PIRSFPIRSF000148. ASA_dh. 1 hit.
SMARTSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR01296. asd_B. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA4J5V7_DESRM
AccessionPrimary (citable) accession number: A4J5V7
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2007
Last sequence update: May 1, 2007
Last modified: May 1, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info