Aspartate-semialdehyde dehydrogenase - Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)

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Q8K9B5 (DHAS_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 79. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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:	BUsg_433

Organism

Buchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]

Taxonomic identifier

198804 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera ›

Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis Methionine biosynthesis Threonine biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	'de novo' L-methionine biosynthetic process Inferred from electronic annotation. Source: HAMAP diaminopimelate biosynthetic process Inferred from electronic annotation. Source: HAMAP isoleucine biosynthetic process Inferred from electronic annotation. Source: InterPro lysine biosynthetic process via diaminopimelate Inferred from electronic annotation. Source: HAMAP threonine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity Inferred from electronic annotation. Source: InterPro NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: HAMAP aspartate-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 371

371

Aspartate-semialdehyde dehydrogenase HAMAP-Rule MF_02121

PRO_0000141364

Regions

Nucleotide binding

11 – 14

NADP By similarity

Nucleotide binding

38 – 39

NADP By similarity

Nucleotide binding

167 – 168

NADP By similarity

Sites

Active site

137

Acyl-thioester intermediate By similarity

Active site

276

Proton acceptor By similarity

Binding site

NADP By similarity

Binding site

104

Phosphate By similarity

Binding site

164

Substrate By similarity

Binding site

243

Substrate By similarity

Binding site

246

Phosphate By similarity

Binding site

269

Substrate By similarity

Binding site

352

NADP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8K9B5 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 079A0E1BEAE68318
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FASTA

371

41,785

        10         20         30         40         50         60 
MTKSVGIIGW RGMVGSVLLK RMQEENDFSK IIPYFFSTSQ SGQDGPIINN ILSKNLKDAY 

        70         80         90        100        110        120 
NINLLQEMDI IITCQGSSYT EKIYPKLRNN NWQGYWIDAA STLRMEKDAT IILDPVNLNV 

       130        140        150        160        170        180 
INNALDKGIK TFVGGNCTVS LMLMALGGLF VNNLIDWVFV STYQAASGAG SRYVIELLKQ 

       190        200        210        220        230        240 
MGSLYNVVSK DLLDKSYSVL DIEKKVTQES RSKNFPLENF SVPLATSLIP WIDVEMKNGQ 

       250        260        270        280        290        300 
SREEWKGQAE TNKILNLKKK VLIDGTCVRI SSIRCHSQSF LIKLNKDISL ENIKKIIVNH 

       310        320        330        340        350        360 
NQWVDVIPNN MQKTLCNLTP SAVTDTLNIP IGRLRKLNID DRYLSAFTVG DQLLWGAAEP 

       370 
LRRMLNLLVN I

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References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013218 Genomic DNA. Translation: AAM67976.1.
RefSeq	NP_660765.1. NC_004061.1.
3D structure databases
ProteinModelPortal	Q8K9B5.
SMR	Q8K9B5. Positions 3-368.
ModBase	Search...
Protein-protein interaction databases
STRING	198804.BUsg433.
Proteomic databases
PRIDE	Q8K9B5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM67976; AAM67976; BUsg_433.
GeneID	1005553.
KEGG	bas:BUsg433.
PATRIC	21247716. VBIBucAph100086_0458.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0136.
KO	K00133.
OMA	SCQGGDY.
ProtClustDB	PRK06598.
Enzyme and pathway databases
BioCyc	BAPH198804:GHMG-456-MONOMER.
UniPathway	UPA00034; UER00016. UPA00050; UER00463. UPA00051; UER00464.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_02121. ASADH.
InterPro	IPR000319. Asp-semialdehyde_DH_CS. IPR011534. Asp_ADH_gamma-type. IPR012080. Asp_semialdehyde_DH. IPR016040. NAD(P)-bd_dom. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_dimer_dom. [Graphical view]
Pfam	PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view]
PIRSF	PIRSF000148. ASA_dh. 1 hit.
SMART	SM00859. Semialdhyde_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR01745. asd_gamma. 1 hit.
PROSITE	PS01103. ASD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHAS_BUCAP

Accession

Primary (citable) accession number: Q8K9B5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	October 1, 2002
Last modified:	May 29, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents