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Q55512 (DHAS_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Aspartate-semialdehyde dehydrogenase

Short name=ASA dehydrogenase
Short name=ASADH
EC=1.2.1.11
Alternative name(s):
Aspartate-beta-semialdehyde dehydrogenase
Gene names
Name:asd
Ordered Locus Names:slr0549
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesSynechocystis

Protein attributes

Sequence length338 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 MF_02121

Catalytic activity

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

Pathway

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

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

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

Subunit structure

Homodimer By similarity. HAMAP MF_02121

Sequence similarities

Belongs to the aspartate-semialdehyde dehydrogenase family.

Sequence caution

The sequence BAA10869.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 338338Aspartate-semialdehyde dehydrogenase HAMAP MF_02121
PRO_0000141393

Regions

Nucleotide binding13 – 164NADP By similarity
Nucleotide binding41 – 422NADP By similarity
Nucleotide binding160 – 1612NADP By similarity

Sites

Active site1301Acyl-thioester intermediate By similarity
Active site2431Proton acceptor By similarity
Binding site1011Phosphate By similarity
Binding site1571Substrate By similarity
Binding site2141Phosphate By similarity
Binding site2361Substrate By similarity
Binding site3161NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q55512 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 6CD73646341EEBB1

FASTA33836,641
        10         20         30         40         50         60 
MPSPIRVAIL GATGAVGTEL LELLASRNFP LAELKLLASP RSAGKTLEFQ GEKLPIQAVD 

        70         80         90        100        110        120 
GSAFKGCDLV LASAGGSTSK RWAEEITKAG AVMVDNSSAF RMVPEVPLVV PEINPEAAQN 

       130        140        150        160        170        180 
HQGIIANPNC TTILMGVAIY PLHQLQPIKR IVVATYQSAS GAGAMAMEEV KHQSRDILEG 

       190        200        210        220        230        240 
KIPQAEILPY PLAFNLFPHN SPITANHYCE EEMKMVQETR KIFAAEDIRI TATCVRVPVL 

       250        260        270        280        290        300 
RAHSEAVNLE FATPFPVELA KTAIAKAPGV KLVEDWQKNY FPMPMDATGQ DDVLVGRIRQ 

       310        320        330 
DISHPNGLDL WLCGDQIRKG AALNAVQIAE LLVERGWL 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome."
Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S.
DNA Res. 2:153-166(1995) [PubMed: 8590279] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27184 / PCC 6803 / N-1.
[2]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27184 / PCC 6803 / N-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA10869.1. Different initiation.
PIRS76022.
RefSeqNP_442798.2. NC_000911.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ55512. 2 interactions.
STRINGQ55512.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID952082.
GenomeReviewsGene locus slr0549 in contig BA000022_GR.
KEGGsyn:slr0549.
NMPDRfig|1148.1.peg.2899.

Phylogenomic databases

eggNOGCOG0136.
HOGENOMHBG518238.
OMALELWLCG.
PhylomeDBQ55512.

Enzyme and pathway databases

BioCycSSP1148:SLR0549-MONOMER.

Family and domain databases

HAMAPMF_02121. ASADH.
[Tree]
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]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00133.
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.
PROSITEPS01103. ASD. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDHAS_SYNY3
AccessionPrimary (citable) accession number: Q55512
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: January 25, 2012
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families