Aspartate-semialdehyde dehydrogenase

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P0A9R1 (DHAS_SHIFL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. History...

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

Documents (2) |

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:	SF3456, S4307

Organism

Shigella flexneri [Complete proteome] [HAMAP]

Taxonomic identifier

623 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	367 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 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 AAN44916.1 differs from that shown. Reason: Erroneous initiation.

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	diaminopimelate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW isoleucine biosynthetic process Inferred from electronic annotation. Source: InterPro methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
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: InterPro aspartate-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: EC protein dimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 367

367

Aspartate-semialdehyde dehydrogenase HAMAP MF_02121

PRO_0000141374

Regions

Nucleotide binding

10 – 13

NADP By similarity

Nucleotide binding

37 – 38

NADP By similarity

Nucleotide binding

165 – 166

NADP By similarity

Sites

Active site

135

Acyl-thioester intermediate By similarity

Active site

274

Proton acceptor By similarity

Binding site

NADP By similarity

Binding site

102

Phosphate By similarity

Binding site

162

Substrate By similarity

Binding site

193

NADP; via carbonyl oxygen By similarity

Binding site

241

Substrate By similarity

Binding site

244

Phosphate By similarity

Binding site

267

Substrate By similarity

Binding site

350

NADP By similarity

Amino acid modifications

Modified residue

135

S-cysteinyl cysteine; in inhibited form By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0A9R1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: F53D4C36EA7CC201
Show »

FASTA

367

40,018

        10         20         30         40         50         60 
MKNVGFIGWR GMVGSVLMQR MVEERDFDAI RPVFFSTSQL GQAAPSFGGT TGTLQDAFDL 

        70         80         90        100        110        120 
EALKALDIIV TCQGGDYTNE IYPKLRESGW QGYWIDAASS LRMKDDAIII LDPVNQDVIT 

       130        140        150        160        170        180 
DGLNNGIRTF VGGNCTVSLM LMSLGGLFAN DLVDWVSVAT YQAASGGGAR HMRELLTQMG 

       190        200        210        220        230        240 
HLYGHVADEL ATPSSAILDI ERKVTTLTRS GELPVDNFGV PLAGSLIPWI DKQLDNGQSR 

       250        260        270        280        290        300 
EEWKGQAETN KILNTSSVIP VDGLCVRVGA LRCHSQAFTI KLKKDVSIPT VEELLAAHNP 

       310        320        330        340        350        360 
WAKVVPNDRE ITMRELTPAA VTGTLTTPVG RLRKLNMGPE FLSAFTVGDQ LLWGAAEPLR 


RMLRQLA

« Hide

References

[1]

"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.

Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.

[2]

"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005674 Genomic DNA. Translation: AAN44916.1. Different initiation. AE014073 Genomic DNA. Translation: AAP19265.1.
RefSeq	NP_709209.2. NC_004337.2. NP_839454.1. NC_004741.1.
3D structure databases
ProteinModelPortal	P0A9R1.
SMR	P0A9R1. Positions 1-367.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000088765; EBESCP00000085587; EBESCG00000087809. EBESCT00000092244; EBESCP00000088880; EBESCG00000091288.
GeneID	1026459. 1080513.
GenomeReviews	Gene locus SF3456 in contig AE005674_GR. Gene locus S4307 in contig AE014073_GR.
KEGG	sfl:SF3456. sfx:S4307.
PATRIC	18710606. VBIShiFle31049_4707.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000010426.
HOGENOM	HBG289760.
ProtClustDB	PRK06598.
Enzyme and pathway databases
BioCyc	SFLE198214:AAN44916.1-MONOMER.
Family and domain databases
HAMAP	MF_02121. ASADH. [Tree]
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]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00133.
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_SHIFL

Accession

Primary (citable) accession number: P0A9R1
Secondary accession number(s): P00353

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 25, 2012
This is version 56 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

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

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure 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