AK2_BACSU
ID AK2_BACSU Reviewed; 408 AA.
AC P08495; P08496; P94554; P97183;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 04-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Aspartokinase 2;
DE EC=2.7.2.4;
DE AltName: Full=Aspartate kinase 2;
DE AltName: Full=Aspartokinase II;
GN Name=lysC; OrderedLocusNames=BSU28470;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3036830; DOI=10.1016/s0021-9258(18)47484-4;
RA Chen N.-Y., Hu F.M., Paulus H.;
RT "Nucleotide sequence of the overlapping genes for the subunits of Bacillus
RT subtilis aspartokinase II and their control regions.";
RL J. Biol. Chem. 262:8787-8798(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA Emmerson P.T., Harwood C.R.;
RT "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT chromosome containing genes responsible for stress responses, the
RT utilization of plant cell walls and primary metabolism.";
RL Microbiology 142:3067-3078(1996).
RN [3]
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 [4]
RP ALTERNATIVE INITIATION.
RX PubMed=2837491; DOI=10.1016/s0021-9258(19)76574-0;
RA Chen N.-Y., Paulus H.;
RT "Mechanism of expression of the overlapping genes of Bacillus subtilis
RT aspartokinase II.";
RL J. Biol. Chem. 263:9526-9532(1988).
RN [5]
RP ACTIVITY REGULATION.
RX PubMed=2168395; DOI=10.1016/s0021-9258(18)77208-6;
RA Graves L.M., Switzer R.L.;
RT "Aspartokinase II from Bacillus subtilis is degraded in response to
RT nutrient limitation.";
RL J. Biol. Chem. 265:14947-14955(1990).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=15033471; DOI=10.1016/j.bbrc.2004.02.122;
RA Kato C., Kurihara T., Kobashi N., Yamane H., Nishiyama M.;
RT "Conversion of feedback regulation in aspartate kinase by domain
RT exchange.";
RL Biochem. Biophys. Res. Commun. 316:802-808(2004).
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:0000269|PubMed:15033471}.
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 Evidence={ECO:0000269|PubMed:15033471};
CC -!- ACTIVITY REGULATION: Lysine-sensitive. Regulated by degradation in
CC response to starvation of cells for various nutrients. Ammonium
CC starvation induced the fastest aspartokinase II decline, followed by
CC amino acid starvation and glucose limitation.
CC {ECO:0000269|PubMed:15033471, ECO:0000269|PubMed:2168395}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.5 mM for ATP {ECO:0000269|PubMed:15033471};
CC KM=10 mM for aspartate {ECO:0000269|PubMed:15033471};
CC Note=kcat is 952 min(-1).;
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
CC regulation) and of a homodimer of 2 isoforms Beta (regulation).
CC {ECO:0000269|PubMed:15033471}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Alpha; Synonyms=Aspartokinase 2 subunit alpha;
CC IsoId=P08495-1; Sequence=Displayed;
CC Name=Beta; Synonyms=Aspartokinase 2 subunit beta;
CC IsoId=P08495-2; Sequence=VSP_018655;
CC -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
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DR EMBL; J03294; AAA87318.1; -; Genomic_DNA.
DR EMBL; J03294; AAA87319.1; -; Genomic_DNA.
DR EMBL; Z75208; CAA99580.1; -; Genomic_DNA.
DR EMBL; Z75208; CAA99581.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14807.1; -; Genomic_DNA.
DR PIR; A29314; A29314.
DR RefSeq; NP_390725.1; NC_000964.3. [P08495-1]
DR RefSeq; WP_003229564.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P08495; -.
DR SMR; P08495; -.
DR IntAct; P08495; 1.
DR MINT; P08495; -.
DR STRING; 224308.BSU28470; -.
DR PaxDb; P08495; -.
DR EnsemblBacteria; CAB14807; CAB14807; BSU_28470.
DR GeneID; 937451; -.
DR KEGG; bsu:BSU28470; -.
DR PATRIC; fig|224308.179.peg.3093; -.
DR eggNOG; COG0527; Bacteria.
DR InParanoid; P08495; -.
DR OMA; IIQSQRC; -.
DR PhylomeDB; P08495; -.
DR BioCyc; BSUB:BSU28470-MON; -.
DR BioCyc; MetaCyc:MON-6561; -.
DR BioCyc; MetaCyc:MON-6562; -.
DR BRENDA; 2.7.2.4; 658.
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 CDD; cd04261; AAK_AKii-LysC-BS; 1.
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; IPR041740; AKii-LysC-BS.
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; PF01842; ACT; 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; 2.
DR PROSITE; PS00324; ASPARTOKINASE; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Amino-acid biosynthesis; ATP-binding;
KW Diaminopimelate biosynthesis; Kinase; Lysine biosynthesis;
KW Nucleotide-binding; Reference proteome; Repeat; Transferase.
FT CHAIN 1..408
FT /note="Aspartokinase 2"
FT /id="PRO_0000002373"
FT DOMAIN 264..337
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 343..408
FT /note="ACT 2"
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 47..49
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125..126
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150..153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 173..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 179..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 289..291
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 354..355
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 368..369
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 375..376
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 7
FT /note="Contribution to the catalysis"
FT /evidence="ECO:0000250"
FT SITE 74
FT /note="Contribution to the catalysis"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..245
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_018655"
FT CONFLICT 166
FT /note="A -> V (in Ref. 1; AAA87318)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 43808 MW; 2E7189F938F97120 CRC64;
MGLIVQKFGG TSVGSVEKIQ NAANRAIAEK QKGHQVVVVV SAMGKSTDEL VSLAKAISDQ
PSKREMDMLL ATGEQVTISL LSMALQEKGY DAVSYTGWQA GIRTEAIHGN ARITDIDTSV
LADQLEKGKI VIVAGFQGMT EDCEITTLGR GGSDTTAVAL AAALKADKCD IYTDVPGVFT
TDPRYVKSAR KLEGISYDEM LELANLGAGV LHPRAVEFAK NYQVPLEVRS STETEAGTLI
EEESSMEQNL IVRGIAFEDQ ITRVTIYGLT SGLTTLSTIF TTLAKRNINV DIIIQTQAED
KTGISFSVKT EDADQTVAVL EEYKDALEFE KIETESKLAK VSIVGSGMVS NPGVAAEMFA
VLAQKNILIK MVSTSEIKVS TVVSENDMVK AVESLHDAFE LSKHPSAV
