Q04797 (DHAS_BACSU) Reviewed, UniProtKB/Swiss-Prot

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:	BSU16750

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	346 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
PTM	Phosphoprotein
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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 346	346	Aspartate-semialdehyde dehydrogenase HAMAP MF_02121		PRO_0000141361
Regions
	Nucleotide binding	13 – 16	4	NADP By similarity
	Nucleotide binding	41 – 42	2	NADP By similarity
	Nucleotide binding	160 – 161	2	NADP By similarity
Sites
	Active site	130	1	Acyl-thioester intermediate By similarity
	Active site	250	1	Proton acceptor By similarity
	Binding site	101	1	Phosphate By similarity
	Binding site	157	1	Substrate By similarity
	Binding site	221	1	Phosphate By similarity
	Binding site	243	1	Substrate By similarity
	Binding site	324	1	NADP 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 [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. Strain: 168.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L08471 Genomic DNA. Translation: AAA22383.1. AL009126 Genomic DNA. Translation: CAB13548.1. Z22554 Genomic DNA. Translation: CAA80276.1.
PIR	F69590.
RefSeq	NP_389557.1. NC_000964.3.
3D structure databases
ProteinModelPortal	Q04797.
SMR	Q04797. Positions 4-346.
ModBase	Search...
PTM databases
PhosSite	Q04797.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000000448; EBBACP00000000448; EBBACG00000000446.
GeneID	939654.
GenomeReviews	Gene locus BSU16750 in contig AL009126_GR.
KEGG	bsu:BSU16750.
NMPDR	fig|224308.1.peg.1678.
PATRIC	18975159. VBIBacSub10457_1771.
Organism-specific databases
GenoList	BSU16750. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000002435.
HOGENOM	HBG518238.
OMA	LELWLCG.
PhylomeDB	Q04797.
ProtClustDB	PRK14874.
Enzyme and pathway databases
BioCyc	BSUB:BSU16750-MONOMER. MetaCyc:MONOMER-6564.
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_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:	January 25, 2012
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program