Aspartate-semialdehyde dehydrogenase

Contribute

Send feedback

Read comments (?) or add your own

P10539 (DHAS_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 99. History...

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

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

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:	SMU_989

Organism

Streptococcus mutans [Complete proteome] [HAMAP]

Taxonomic identifier

1309 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	358 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 – 358

358

Aspartate-semialdehyde dehydrogenase HAMAP MF_02121

PRO_0000141392

Regions

Nucleotide binding

11 – 14

NADP By similarity

Nucleotide binding

39 – 40

NADP By similarity

Nucleotide binding

158 – 159

NADP By similarity

Sites

Active site

128

Acyl-thioester intermediate By similarity

Active site

252

Proton acceptor By similarity

Binding site

Phosphate By similarity

Binding site

155

Substrate By similarity

Binding site

223

Phosphate By similarity

Binding site

245

Substrate By similarity

Binding site

325

NADP By similarity

Experimental info

Sequence conflict

G → A in AAA26850. Ref.1

Sequence conflict

190

L → F in AAA26850. Ref.1

Sequence conflict

242

T → H in AAA26850. Ref.1

Sequence conflict

301

Missing in AAA26850. Ref.1

Sequence conflict

335 – 340

VQIAES → IITANR in AAA26850. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P10539 [UniParc].

Last modified November 28, 2002. Version 2.
Checksum: 11F5E4AD52C1A40B
Show »

FASTA

358

38,903

        10         20         30         40         50         60 
MGYTVAIVGA TGAVGTRMIQ QLEQSTLPVD KVRLLSSSRS AGKVLQYKDQ DVTVELTTKD 

        70         80         90        100        110        120 
SFEGVDIALF SAGGSVSAKF APYAVKAGAV VVDNTSHFRQ NPDVPLVVPE VNAYAMDAHN 

       130        140        150        160        170        180 
GIIACPNCST IQMMVALEPI RQKWGLSRVI VSTYQAVSGA GQSAINETVR EIKEVVNDGV 

       190        200        210        220        230        240 
DPKAVHADIL PSGGDKKHYP IAFNALAQID VFTDNDYTYE EMKMTNETKK IMEEPELPVS 

       250        260        270        280        290        300 
ATCVRVPILF SHSEAVYIET KDVAPIEEVK AAIAAFPGAV LEDDIKHQIY PQAANAVGSR 

       310        320        330        340        350 
ETFVGRIRKD LDIENGIHMW VVSDNLLKGA AWNSVQIAES LHERGLVRST SELKFELK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the asd gene of Streptococcus mutans. Identification of the promoter region and evidence for attenuator-like sequences preceding the structural gene." Cardineau G.A., Curtiss R. III J. Biol. Chem. 262:3344-3353(1987) [PubMed: 2434499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen." Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J. Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed: 12397186] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700610 / UA159 / Serotype c.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J02667 Genomic DNA. Translation: AAA26850.1. AE014133 Genomic DNA. Translation: AAN58690.1.
PIR	A29137.
RefSeq	NP_721384.1. NC_004350.2.
3D structure databases
ProteinModelPortal	P10539.
SMR	P10539. Positions 2-358.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTRT00000013844; EBSTRP00000013326; EBSTRG00000013844.
GeneID	1028321.
GenomeReviews	Gene locus SMU_989 in contig AE014133_GR.
KEGG	smu:SMU_989.
NMPDR	fig\|210007.1.peg.897.
PATRIC	19664099. VBIStrMut61772_0882.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000027605.
HOGENOM	HBG518238.
OMA	FHGKQVE.
ProtClustDB	PRK14874.
Enzyme and pathway databases
BioCyc	SMUT210007:SMU_989-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_STRMU

Accession

Primary (citable) accession number: P10539

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 28, 2002
Last modified:	January 25, 2012
This is version 99 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

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents