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A5FZ89 (A5FZ89_ACICJ) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:Acry_1717 EMBL ABQ30921.1
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP] EMBL ABQ30921.1
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcidiphilium

Protein attributes

Sequence length347 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 binding11 – 144NADP By similarity HAMAP-Rule MF_02121
Nucleotide binding39 – 402NADP By similarity HAMAP-Rule MF_02121
Nucleotide binding165 – 1662NADP By similarity HAMAP-Rule MF_02121

Sites

Active site1351Acyl-thioester intermediate By similarity HAMAP-Rule MF_02121 PIRSR PIRSR000148-1
Active site2471Proton acceptor By similarity HAMAP-Rule MF_02121 PIRSR PIRSR000148-1
Binding site1001Phosphate By similarity HAMAP-Rule MF_02121
Binding site1621Substrate By similarity HAMAP-Rule MF_02121
Binding site2161Substrate By similarity HAMAP-Rule MF_02121
Binding site2191Phosphate By similarity HAMAP-Rule MF_02121
Binding site2401Substrate By similarity HAMAP-Rule MF_02121
Binding site3201NADP By similarity HAMAP-Rule MF_02121

Sequences

Sequence LengthMass (Da)Tools
A5FZ89 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: F85F82E6690F6117

FASTA34737,519
        10         20         30         40         50         60 
MAYKVAVVGA TGAVGREMLK TLAERNFPAS EVIALASPRS AGQQVSFGDE AILTVKNLET 

        70         80         90        100        110        120 
FDFRGVDFGL FSPGASISAV HAPRAAEAGC IVIDNTSHFR MEPDVPLVVP EVNTHALEAF 

       130        140        150        160        170        180 
MAKPDWRRII ANPNCSTIQM VVALKPLHEK FGIRRVSVAT YQSVSGAGKE GMDELERATK 

       190        200        210        220        230        240 
ATYVHETTKP EVFTKPIAFN VIPHIDVFMK DGATKEEWKM TVETRKILDP DIAVFATCVR 

       250        260        270        280        290        300 
VPVFIGHGEA VHVEFANPAP LEAARAALRA APGVTLFDER EDGGYVTPLE CQGEDAVYVS 

       310        320        330        340 
RLRVDPTVPH GLGFWCVSDN LRKGAALNAV QIAETIVKRG LIGKKAA 

« Hide

References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
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., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JF-5 EMBL ABQ30921.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000697 Genomic DNA. Translation: ABQ30921.1.
RefSeqYP_001234840.1. NC_009484.1.

3D structure databases

ProteinModelPortalA5FZ89.
SMRA5FZ89. Positions 2-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349163.Acry_1717.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ30921; ABQ30921; Acry_1717.
GeneID5161283.
KEGGacr:Acry_1717.
PATRIC20648472. VBIAciCry6074_2217.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0136.
HOGENOMHOG000013357.
KOK00133.
OMAFPIKKFV.
OrthoDBEOG6JB158.
ProtClustDBPRK14874.

Enzyme and pathway databases

BioCycACRY349163:GHET-1743-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 nameA5FZ89_ACICJ
AccessionPrimary (citable) accession number: A5FZ89
Entry history
Integrated into UniProtKB/TrEMBL: June 12, 2007
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)