Reviewed, UniProtKB/Swiss-Prot Q04797 (DHAS_BACSU)

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:	BSU16750

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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
PTM	Phosphoprotein
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 – 346	346	Aspartate-semialdehyde dehydrogenase		PRO_0000141361
Sites
	Active site	130	1	Acyl-thioester intermediate By similarity
Amino acid modifications
	Modified residue	98	1	Phosphoserine Ref.4
	Modified residue	146	1	Phosphotyrosine Ref.4
Experimental info
	Sequence conflict	42	1	S → A in CAA80276. Ref.3
	Sequence conflict	77	1	S → T in CAA80276. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q04797-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: C3548164085143CD	FASTA	346	37,847
	10 20 30 40 50 60 MGRGLHVAVV GATGAVGQQM LKTLEDRNFE MDTLTLLSSK RSAGTKVTFK GQELTVQEAS 70 80 90 100 110 120 PESFEGVNIA LFSAGGSVSQ ALAPEAVKRG AIVIDNTSAF RMDENTPLVV PEVNEADLHE 130 140 150 160 170 180 HNGIIANPNC STIQMVAALE PIRKAYGLNK VIVSTYQAVS GAGNEAVKEL YSQTQAILNK 190 200 210 220 230 240 EEIEPEIMPV KGDKKHYQIA FNAIPQIDKF QDNGYTFEEM KMINETKKIM HMPDLQVAAT 250 260 270 280 290 300 CVRLPIQTGH SESVYIEIDR DDATVEDIKN LLKEAPGVTL QDDPSQQLYP MPADAVGKND 310 320 330 340 VFVGRIRKDL DRANGFHLWV VSDNLLKGAA WNSVQIAESL KKLNLV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase." Chen N.-Y., Jiang S.-Q., Klein D.A., Paulus H. J. Biol. Chem. 268:9448-9465(1993) [PubMed: 8098035] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Cloning, DNA sequence, functional analysis and transcriptional regulation of the genes encoding dipicolinic acid synthetase required for sporulation in Bacillus subtilis." Daniel R.A., Errington J. J. Mol. Biol. 232:468-483(1993) [PubMed: 8345520] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-208.
[4]	"The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis." Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M. Mol. Cell. Proteomics 6:697-707(2007) [PubMed: 17218307] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND TYR-146, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L08471 Genomic DNA. Translation: AAA22383.1. AL009126 Genomic DNA. Translation: CAB13548.1. Z22554 Genomic DNA. Translation: CAA80276.1.
PIR	F69590.
RefSeq	NP_389557.1.
3D structure databases
ModBase	Search...
PTM databases
PhosSite	Q04797.
Genome annotation databases
GeneID	939654.
GenomeReviews	Gene locus BSU16750 in contig AL009126_GR.
KEGG	bsu:BSU16750.
NMPDR	fig|224308.1.peg.1678.
Organism-specific databases
SubtiList	BG10783. asd. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	Q04797.
OMA	Q04797. LELWLCG.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1676-MON. MetaCyc:MON-6564.
BRENDA	1.2.1.11. 150.
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_BACSU

Accession

Primary (citable) accession number: Q04797

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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