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UniProtKB/Swiss-Prot entry Q04797


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DHAS_BACSU
Primary accession number Q04797
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on October 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 68)
Name and origin of the protein
Protein name Aspartate-semialdehyde dehydrogenase
Synonyms ASA dehydrogenase
ASADH
EC 1.2.1.11
Gene name
Name: asd
OrderedLocusNames: BSU16750
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=8098035 [NCBI, ExPASy, EBI, Israel, Japan]
Chen N.-Y., Jiang S.-Q., Klein D.A., Paulus H.;
"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.";
J. Biol. Chem. 268:9448-9465(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis.";
Nature 390:249-256(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-208.
DOI=10.1006/jmbi.1993.1403; PubMed=8345520 [NCBI, ExPASy, EBI, Israel, Japan]
Daniel R.A., Errington J.;
"Cloning, DNA sequence, functional analysis and transcriptional regulation of the genes encoding dipicolinic acid synthetase required for sporulation in Bacillus subtilis.";
J. Mol. Biol. 232:468-483(1993).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND TYR-146, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M600464-MCP200; PubMed=17218307 [NCBI, ExPASy, EBI, Israel, Japan]
Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.;
"The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.";
Mol. Cell. Proteomics 6:697-707(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L08471; AAA22383.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99112; CAB13548.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z22554; CAA80276.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR F69590; F69590.
RefSeq NP_389557.1; -.
3D structure databases
ModBase Q04797.
Enzyme and pathway databases
BioCyc BSUB224308:BSU1676-MON; -.
MetaCyc:MON-6564; -.
Organism-specific databases
SubtiList BG10783; asd. [Micado]
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0004073; Molecular function: aspartate-semialdehyde dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0046983; Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0019877; Biological process: diaminopimelate biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0009086; Biological process: methionine biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009088; Biological process: threonine biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000319; Asp-semialdehyde_DHase_CS.
IPR012080; Asp_semialdehyde_DHase.
IPR005986; Asp_semialdehyde_DHase_bac.
IPR000534; Semialdehyde_DHase_NAD-bd.
IPR012280; Semialdhyde_DHase_C.
Graphical view of domain structure.
Pfam PF01118; Semialdhyde_dh; 1.
PF02774; Semialdhyde_dhC; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000148; ASA_dh; 1.
TIGRFAMs TIGR01296; asd_B; 1.
PROSITE PS01103; ASD; 1.
Genome annotation databases
GeneID 939654; -.
GenomeReviews AL009126_GR; BSU16750.
KEGG bsu:BSU16750; -.
NMPDR fig|224308.1.peg.1678; -.
Phylogenomic databases
HOGENOM Q04797; -.
Genome annotation databases
CMR Q04797; BSU16750.
Other
ProtoNet Q04797.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Diaminopimelate biosynthesis; Lysine biosynthesis; NADP; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   346  346     Aspartate-semialdehyde dehydrogenase. PRO_0000141361
ACT_SITE   130   130        Acyl-thioester intermediate (By similarity). 
MOD_RES   98    98        Phosphoserine. 
MOD_RES   146   146        Phosphotyrosine. 
CONFLICT   42    42        S -> A (in Ref. 3; CAA80276). 
CONFLICT   77    77        S -> T (in Ref. 3; CAA80276). 
Sequence information
Length: 346 AA [This is the length of the unprocessed precursor] Molecular weight: 37847 Da [This is the MW of the unprocessed precursor] CRC64: C3548164085143CD [This is a checksum on the sequence]
        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 

Q04797 in FASTA format

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View entry in raw text format (no links)
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