Reviewed, UniProtKB/Swiss-Prot P10539 (DHAS_STRMU)

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:	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.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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.

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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 358	358	Aspartate-semialdehyde dehydrogenase		PRO_0000141392
Sites
	Active site	128	1	Acyl-thioester intermediate By similarity
Experimental info
	Sequence conflict	64	1	G → A in AAA26850. Ref.1
	Sequence conflict	190	1	L → F in AAA26850. Ref.1
	Sequence conflict	242	1	T → H in AAA26850. Ref.1
	Sequence conflict	301	1	Missing in AAA26850. Ref.1
	Sequence conflict	335 – 340	6	VQIAES → IITANR in AAA26850. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P10539-1 [UniParc]. Last modified November 28, 2002. Version 2. Checksum: 11F5E4AD52C1A40B	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

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
EMBLGenBankDDBJ	J02667 Genomic DNA. Translation: AAA26850.1. AE014133 Genomic DNA. Translation: AAN58690.1.
PIR	A29137.
RefSeq	NP_721384.1.
3D structure databases
HSSP	HSSP built from PDB template 1BRM based on UniProtKB P00353.
SMR	P10539. Positions 2-358.
ModBase	Search...
Genome annotation databases
GeneID	1028321.
GenomeReviews	Gene locus SMU_989 in contig AE014133_GR.
KEGG	smu:SMU.989.
NMPDR	fig|210007.1.peg.897.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P10539.
OMA	P10539. VFYGHAE.
Enzyme and pathway databases
BioCyc	SMUT210007:SMU_989-MON.
BRENDA	1.2.1.11. 20716.
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...

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:	June 16, 2009
This is version 76 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)