Aspartate-semialdehyde dehydrogenase

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Reviewed, UniProtKB/Swiss-Prot Q59291 (DHAS_CAMJE)

Last modified June 16, 2009. Version 62. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Aspartate-semialdehyde dehydrogenase
      Short name=ASA dehydrogenase
      Short name=ASADH
    EC=1.2.1.11

Gene names

Name:	asd
Ordered Locus Names:	Cj1023c

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

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Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	L-aspartate 4-semialdehyde + phosphate + NADP⁺ = L-4-aspartyl phosphate + NADPH.
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; tetrahydrodipicolinate from L-aspartate: step 2/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the aspartate-semialdehyde dehydrogenase family.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine 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 methionine biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW threonine biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADP or NADPH 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...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
flaG	Q0PAW9	1	EBI-1193698,EBI-1191365
fliY	Q0PC74	1	EBI-1193698,EBI-1191111

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 343

343

Aspartate-semialdehyde dehydrogenase

PRO_0000141366

Sites

Active site

134

Acyl-thioester intermediate By similarity

Experimental info

Sequence conflict

43 – 56

VGSEV…KAYKV → AGNQIEFRGKSYTI Ref.1

Sequence conflict

62 – 65

NVFK → DAFR in CAA66607. Ref.1

Sequence conflict

I → V in CAA66607. Ref.1

Sequence conflict

S → A in CAA66607. Ref.1

Sequence conflict

106

K → E in CAA66607. Ref.1

Sequence conflict

122

D → E in CAA66607. Ref.1

Sequence conflict

141 – 142

QV → HI in CAA66607. Ref.1

Sequence conflict

151

N → D in CAA66607. Ref.1

Sequence conflict

172

Q → E in CAA66607. Ref.1

Sequence conflict

176

E → R in CAA66607. Ref.1

Sequence conflict

191

P → A in CAA66607. Ref.1

Sequence conflict

196

Y → H in CAA66607. Ref.1

Sequence conflict

213

D → G in CAA66607. Ref.1

Sequence conflict

222

V → I in CAA66607. Ref.1

Sequence conflict

235

V → I in CAA66607. Ref.1

Sequence conflict

257

E → A in CAA66607. Ref.1

Sequence conflict

260

I → V in CAA66607. Ref.1

Sequence conflict

263

K → N in CAA66607. Ref.1

Sequence conflict

266 – 267

KE → RD in CAA66607. Ref.1

Sequence conflict

270 – 271

KK → QN in CAA66607. Ref.1

Sequence conflict

276

I → V in CAA66607. Ref.1

Sequence conflict

280

D → E in CAA66607. Ref.1

Sequence conflict

283

N → D in CAA66607. Ref.1

Sequence conflict

305

A → L in CAA66607. Ref.1

Sequence conflict

308 – 311

YDKK → THKN in CAA66607. Ref.1

Sequence conflict

341

K → E in CAA66607. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

Q59291-1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: D122507423187E26
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FASTA

343

38,375

        10         20         30         40         50         60 
MSKKQKIAIV GATGAVGEEL LNVLDELDFP VESILPLASA KSVGSEVEFK GKAYKVKELT 

        70         80         90        100        110        120 
ENVFKENPID IAFFSAGGSV SEKYAKFAVE SGAVVIDNTS HFRMEKDVPL VVPECNPEDI 

       130        140        150        160        170        180 
KDWKKTGIIA NPNCSTIQMV QVLKPLNDAF NLKRVDVSTY QAASGAGKEG MQELVEAMQS 

       190        200        210        220        230        240 
FFAFKLDEFE PQTFPYTLAL NLIPQIDVFM DNDYTKEELK MVNETQKILH KNLEVSATCV 

       250        260        270        280        290        300 
RVPVLRSHSE AITMHFEKEI DVKKAKEILK KAPSVIVIDD PKNKKYPMPL MTSDTNETYV 

       310        320        330        340 
GRIRADVYDK KILHLWCVAD QIRVGAATNA VRIAQKWLEL KNK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete nucleotide sequence of the Campylobacter jejuni 72Dz asd gene." Pawelec D., Jagusztyn-Krynicka E.K. Acta Microbiol. Pol. 45:299-304(1996) [PubMed: 9127485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DZ72/92.
[2]	"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

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Cross-references

Sequence databases
	X97964 Genomic DNA. Translation: CAA66607.1. AL111168 Genomic DNA. Translation: CAL35141.1.
PIR	D81304.
RefSeq	YP_002344418.1.
3D structure databases
HSSP	HSSP built from PDB template 1BRM based on UniProtKB P00353.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q59291. 62 interactions.
Genome annotation databases
GeneID	905315.
GenomeReviews	Gene locus Cj1023c in contig AL111168_GR.
KEGG	cje:Cj1023c.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	Q59291. VFYGHAE.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ1023C-MON.
BRENDA	1.2.1.11. 255835.
Family and domain databases
InterPro	IPR000319. Asp-semialdehyde_DH_CS. IPR012080. Asp_semialdehyde_DH. IPR005986. Asp_semialdehyde_DH_bac. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_C. [Graphical view]
Pfam	PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view]
PIRSF	PIRSF000148. ASA_dh. 1 hit.
TIGRFAMs	TIGR01296. asd_B. 1 hit.
PROSITE	PS01103. ASD. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

DHAS_CAMJE

Accession

Primary (citable) accession number: Q59291
Secondary accession number(s): Q0P9M9, Q9PNR7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 1, 2000
Last modified:	June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents