Aspartate-semialdehyde dehydrogenase - Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12)

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Q56734 (DHAS_SHEVD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 77. 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:	SVI_2879

Organism

Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12) [Complete proteome] [HAMAP]

Taxonomic identifier

637905 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella

Protein attributes

Sequence length	338 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.

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 – 338

338

Aspartate-semialdehyde dehydrogenase HAMAP MF_02121

PRO_0000141390

Regions

Nucleotide binding

13 – 16

NADP By similarity

Nucleotide binding

41 – 42

NADP By similarity

Nucleotide binding

162 – 163

NADP By similarity

Sites

Active site

132

Acyl-thioester intermediate By similarity

Active site

245

Proton acceptor By similarity

Binding site

101

Phosphate By similarity

Binding site

159

Substrate By similarity

Binding site

216

Phosphate By similarity

Binding site

238

Substrate By similarity

Binding site

317

NADP By similarity

Experimental info

Sequence conflict

181

Q → H in BAA08490. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q56734 [UniParc].

Last modified August 10, 2010. Version 2.
Checksum: 6269F1E22CC5D359
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FASTA

338

37,052

        10         20         30         40         50         60 
MSQEFNVVVL GASGAVGQTM IEILEERNFP VAKLFPLASS RSAGGTVSFN GKQVEILDVD 

        70         80         90        100        110        120 
DFDWSQAQIG FFSAGGDVSE KWAPIAAENG CVVIDNTSQF RYDNDVPLVI PEVNPEAIAD 

       130        140        150        160        170        180 
FRNRNIIANP NCSTIQMLVA LKPIYDAFGI SRINVATYQS VSGSGKEAIT ELAGQCSKLL 

       190        200        210        220        230        240 
QGLPAESKVY PKQIAFNVLP QIDKFMENGY TKEEMKMVWE TQKIFGDDNI VVNPTAVRVP 

       250        260        270        280        290        300 
VFYGHSEAIH LETIQPAEAE DVKAVLREAP GIELFESNEE YPTAVTESAG TDPVYVGRVR 

       310        320        330 
KDISHSHGIN LWVVSDNIRK GAALNSVQIA EVLIRDYY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparison of the gene expression of aspartate beta-D-semialdehyde dehydrogenase at elevated hydrostatic pressure in deep-sea bacteria." Kato C., Smorawinska M., Li L., Horikoshi K. J. Biochem. 121:717-723(1997) [PubMed: 9163523] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence and comparative analysis of Shewanella violacea, a psychrophilic and piezophilic bacterium from deep sea floor sediments." Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H., Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T., Nakasone K., Mori H. Mol. Biosyst. 6:1216-1226(2010) [PubMed: 20458400] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JCM 10179 / CIP 106290 / LMG 19151 / DSS12.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D49540 Genomic DNA. Translation: BAA08490.1. AP011177 Genomic DNA. Translation: BAJ02850.1.
PIR	JC5436.
RefSeq	YP_003557628.1. NC_014012.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	8966956.
GenomeReviews	Gene locus SVI_2879 in contig AP011177_GR.
KEGG	svo:SVI_2879.
PATRIC	35461951. VBISheVio92117_2772.
Organism-specific databases
CMR	Search...
Phylogenomic databases
ProtClustDB	CLSK906983.
Family and domain databases
HAMAP	MF_02121. ASADH. [Tree]
InterPro	IPR012080. 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]
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	TIGR01296. Asd_B. 1 hit.
PROSITE	PS01103. ASD. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHAS_SHEVD

Accession

Primary (citable) accession number: Q56734
Secondary accession number(s): D4ZMF1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 10, 2010
Last modified:	January 25, 2012
This is version 77 of the entry and version 2 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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents