AK1_BACSU
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 03-AUG-2022, entry version 158.
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; DOI=10.1016/s0021-9258(18)98372-9;
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 enzymes
RT 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., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., 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., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., 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., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
CC -!- FUNCTION: Catalyzes the phosphorylation of the beta-carboxyl group of
CC 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 {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP;
CC Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
CC -!- ACTIVITY 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 novo
CC pathway; L-homoserine from L-aspartate: step 1/3.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5.
CC -!- SUBUNIT: Tetramer consisting of 2 isoforms Alpha (catalytic) and 2
CC isoforms Beta (function not known). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 RefSeq; WP_003245524.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; Q04795; -.
DR SMR; Q04795; -.
DR IntAct; Q04795; 1.
DR MINT; Q04795; -.
DR STRING; 224308.BSU16760; -.
DR jPOST; Q04795; -.
DR PaxDb; Q04795; -.
DR PRIDE; Q04795; -.
DR EnsemblBacteria; CAB13549; CAB13549; BSU_16760.
DR GeneID; 936710; -.
DR KEGG; bsu:BSU16760; -.
DR PATRIC; fig|224308.179.peg.1818; -.
DR eggNOG; COG0527; Bacteria.
DR InParanoid; Q04795; -.
DR OMA; LMSCGEV; -.
DR PhylomeDB; Q04795; -.
DR BioCyc; BSUB:BSU16760-MON; -.
DR BioCyc; MetaCyc:BSU16760-MON; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004072; F:aspartate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009090; P:homoserine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR005260; Asp_kin_monofn.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR018042; Aspartate_kinase_CS.
DR InterPro; IPR027795; CASTOR_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 SUPFAM; SSF55021; SSF55021; 2.
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 Diaminopimelate biosynthesis; Kinase; Lysine biosynthesis;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..404
FT /note="Aspartokinase 1"
FT /id="PRO_0000002367"
FT DOMAIN 344..404
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT BINDING 7..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 25..30
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 52..54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 130..131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155..158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 178..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 184..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 299..301
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 355..356
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 369..370
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 376..377
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 7
FT /note="Contribution to the catalysis"
FT /evidence="ECO:0000250"
FT SITE 79
FT /note="Contribution to the catalysis"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..244
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_018652"
FT VAR_SEQ 245
FT /note="V -> M (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="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
