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Database: UniProt
Entry: Q04795
LinkDB: Q04795
Original site: Q04795 
ID   AK1_BACSU               Reviewed;         404 AA.
AC   Q04795; O31759;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   09-JUL-2014, entry version 117.
DE   RecName: Full=Aspartokinase 1;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartate kinase 1;
DE   AltName: Full=Aspartokinase I;
GN   Name=dapG; Synonyms=lssD; OrderedLocusNames=BSU16760;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8098035;
RA   Chen N.-Y., Jiang S.-Q., Klein D.A., Paulus H.;
RT   "Organization and nucleotide sequence of the Bacillus subtilis
RT   diaminopimelate operon, a cluster of genes encoding the first three
RT   enzymes of diaminopimelate synthesis and dipicolinate synthase.";
RL   J. Biol. Chem. 268:9448-9465(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 399.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
RA   Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus
RT   subtilis 168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- FUNCTION: Catalyzes the phosphorylation of the beta-carboxyl group
CC       of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is
CC       involved in the branched biosynthetic pathway leading to the
CC       biosynthesis of amino acids threonine, isoleucine and methionine
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-
CC       aspartate.
CC   -!- ENZYME REGULATION: Diaminopimelate-sensitive.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 1/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 1/5.
CC   -!- SUBUNIT: Tetramer consisting of 2 isoforms Alpha (catalytic) and 2
CC       isoforms Beta (function not known) (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Alpha; Synonyms=Aspartokinase 1 subunit alpha;
CC         IsoId=Q04795-1; Sequence=Displayed;
CC       Name=Beta; Synonyms=Aspartokinase 1 subunit beta;
CC         IsoId=Q04795-2; Sequence=VSP_018652, VSP_018985;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC   -!- SIMILARITY: Contains 1 ACT domain.
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DR   EMBL; L08471; AAA22384.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13549.2; -; Genomic_DNA.
DR   PIR; C46665; C46665.
DR   RefSeq; NP_389558.2; NC_000964.3. [Q04795-1]
DR   ProteinModelPortal; Q04795; -.
DR   SMR; Q04795; 1-403.
DR   IntAct; Q04795; 1.
DR   MINT; MINT-8366666; -.
DR   STRING; 224308.BSU16760; -.
DR   PaxDb; Q04795; -.
DR   EnsemblBacteria; CAB13549; CAB13549; BSU16760.
DR   GeneID; 936710; -.
DR   KEGG; bsu:BSU16760; -.
DR   PATRIC; 18975161; VBIBacSub10457_1772.
DR   GenoList; BSU16760; -.
DR   eggNOG; COG0527; -.
DR   HOGENOM; HOG000293093; -.
DR   KO; K00928; -.
DR   OrthoDB; EOG6NSGHC; -.
DR   PhylomeDB; Q04795; -.
DR   BioCyc; BSUB:BSU16760-MONOMER; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR005260; Asp_kin_monofn.
DR   InterPro; IPR001341; Asp_kinase_dom.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   InterPro; IPR027795; GATS-like_ACT_dom.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF13840; ACT_7; 1.
DR   PIRSF; PIRSF000726; Asp_kin; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00656; asp_kin_monofn; 1.
DR   TIGRFAMs; TIGR00657; asp_kinases; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   3: Inferred from homology;
KW   Alternative initiation; Amino-acid biosynthesis; ATP-binding;
KW   Complete proteome; Diaminopimelate biosynthesis; Kinase;
KW   Lysine biosynthesis; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN         1    404       Aspartokinase 1.
FT                                /FTId=PRO_0000002367.
FT   DOMAIN      344    404       ACT.
FT   REGION        7     10       ATP binding (By similarity).
FT   REGION       25     30       Substrate binding (By similarity).
FT   REGION       52     54       Substrate binding (By similarity).
FT   REGION      130    131       Substrate binding (By similarity).
FT   REGION      155    158       Substrate binding (By similarity).
FT   REGION      178    179       ATP binding (By similarity).
FT   REGION      184    189       ATP binding (By similarity).
FT   REGION      299    301       Substrate binding (By similarity).
FT   REGION      355    356       Substrate binding (By similarity).
FT   REGION      369    370       Substrate binding (By similarity).
FT   REGION      376    377       Substrate binding (By similarity).
FT   BINDING      41     41       ATP (By similarity).
FT   BINDING      79     79       Substrate (By similarity).
FT   BINDING     158    158       Substrate (By similarity).
FT   SITE          7      7       Contribution to the catalysis (By
FT                                similarity).
FT   SITE         79     79       Contribution to the catalysis (By
FT                                similarity).
FT   VAR_SEQ       1    244       Missing (in isoform Beta).
FT                                /FTId=VSP_018652.
FT   VAR_SEQ     245    245       V -> M (in isoform Beta).
FT                                /FTId=VSP_018985.
SQ   SEQUENCE   404 AA;  42948 MW;  49A6DA70D71997C4 CRC64;
     MKIIVQKFGG TSVKDDKGRK LALGHIKEAI SEGYKVVVVV SAMGRKGDPY ATDSLLGLLY
     GDQSAISPRE QDLLLSCGET ISSVVFTSML LDNGVKAAAL TGAQAGFLTN DQHTNAKIIE
     MKPERLFSVL ANHDAVVVAG FQGATEKGDT TTIGRGGSDT SAAALGAAVD AEYIDIFTDV
     EGVMTADPRV VENAKPLPVV TYTEICNLAY QGAKVISPRA VEIAMQAKVP IRVRSTYSND
     KGTLVTSHHS SKVGSDVFER LITGIAHVKD VTQFKVPAKI GQYNVQTEVF KAMANAGISV
     DFFNITPSEI VYTVAGNKTE TAQRILMDMG YDPMVTRNCA KVSAVGAGIM GVPGVTSKIV
     SALSEKEIPI LQSADSHTTI WVLVHEADMV PAVNALHEVF ELSK
//
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