Aspartate-semialdehyde dehydrogenase

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Q59291 (DHAS_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 84. History...

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

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·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:	Cj1023c

Organism

Campylobacter jejuni

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	343 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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 Reference 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...

Binary interactions

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 343

343

Aspartate-semialdehyde dehydrogenase HAMAP MF_02121

PRO_0000141366

Regions

Nucleotide binding

13 – 16

NADP By similarity

Nucleotide binding

41 – 42

NADP By similarity

Nucleotide binding

164 – 165

NADP By similarity

Sites

Active site

134

Acyl-thioester intermediate By similarity

Active site

248

Proton acceptor By similarity

Binding site

103

Phosphate By similarity

Binding site

161

Substrate By similarity

Binding site

220

Phosphate By similarity

Binding site

241

Substrate By similarity

Binding site

321

NADP 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

Sequences

Sequence

Length

Mass (Da)

Tools

Q59291 [UniParc].

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

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

« Hide

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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X97964 Genomic DNA. Translation: CAA66607.1. AL111168 Genomic DNA. Translation: CAL35141.1.
PIR	D81304.
RefSeq	YP_002344418.1. NC_002163.1.
3D structure databases
ProteinModelPortal	Q59291.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q59291. 63 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	905315.
GenomeReviews	Gene locus Cj1023c in contig AL111168_GR.
KEGG	cje:Cj1023c.
PATRIC	20059004. VBICamJej33762_1005.
Phylogenomic databases
HOGENOM	HBG518238.
OMA	FHGKQVE.
ProtClustDB	PRK14874.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ1023C-MONOMER.
Family and domain databases
HAMAP	MF_02121. ASADH. [Tree]
InterPro	IPR000319. Asp-semialdehyde_DH_CS. 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. 1 hit. [Graphical view]
ProtoNet	Search...

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:	January 25, 2012
This is version 84 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents