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 01-MAY-2013, entry version 108.
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.
DR ProteinModelPortal; Q04795; -.
DR SMR; Q04795; 1-403.
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 ProtClustDB; PRK08210; -.
DR BioCyc; BSUB:BSU16760-MONOMER; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR GO; GO:0004072; F:aspartate kinase activity; IEA: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; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR005260; Asp_kin_monofn.
DR InterPro; IPR001341; Asp_kinase_dom.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF000726; Asp_kin; 1.
DR SUPFAM; SSF53633; Aa_kinase; 1.
DR TIGRFAMs; TIGR00656; asp_kin_monofn; 1.
DR TIGRFAMs; TIGR00657; asp_kinases; 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 286 336 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
//
