AK_GEOSE
ID AK_GEOSE Reviewed; 407 AA.
AC P53553;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Aspartokinase;
DE EC=2.7.2.4;
DE AltName: Full=Aspartate kinase;
GN Name=lysC;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NUB3621;
RX PubMed=8635739; DOI=10.1016/0378-1119(95)00834-9;
RA Cantoni R., Labo M., de Rossi E., Riccardi G.;
RT "Sequence of the Bacillus stearothermophilus gene encoding aspartokinase
RT II.";
RL Gene 169:135-136(1996).
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: Lysine-sensitive. {ECO:0000250}.
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:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Alpha; Synonyms=Aspartokinase 2 subunit alpha;
CC IsoId=P53553-1; Sequence=Displayed;
CC Name=Beta; Synonyms=Aspartokinase 2 subunit beta;
CC IsoId=P53553-2; Sequence=VSP_018654;
CC -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
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DR EMBL; L46351; AAB06216.1; -; Genomic_DNA.
DR PIR; JC4640; JC4640.
DR AlphaFoldDB; P53553; -.
DR SMR; P53553; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
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: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 3: Inferred from homology;
KW Alternative initiation; Amino-acid biosynthesis; ATP-binding;
KW Diaminopimelate biosynthesis; Kinase; Lysine biosynthesis;
KW Nucleotide-binding; Repeat; Transferase.
FT CHAIN 1..407
FT /note="Aspartokinase"
FT /id="PRO_0000002371"
FT DOMAIN 264..338
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 340..407
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 351..352
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 365..366
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 372..373
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_018654"
SQ SEQUENCE 407 AA; 44002 MW; 2A848E6A7037B172 CRC64;
MGIIVQKFGG TSVGSIERIQ HVANRVIEEV QKGNDVVVVV SAMGKTTDEL VNLAKQISNH
PSKREMDMLL STGEQVSIAL LAMSLHEKGY KAVSLTGWQA GITTEEMHGN ARIMNIDTTR
IRRCLDEGAI VIVAGFQGVT ETGEITTLGR GGSDTTAVAL AAALKAEKCD IYTDVTGVFT
TDPRYVKTAR KIKEISYDEM LELANLGAGV LHPRAVEFAK NYEVPLEVRS SMENERGTMV
KEEVSMEQHL IVRGIAFEDQ VTRVTVVGIE KYLQSVATIF TALANRGINV DIIIQNATNS
ETASVSFSIR TEDLPETLQV LQALEGADVH YESGLAKVSI VGSGMISNPG VAARVFEVLA
DQGIEIKMVS ISEIKISTVI DEKYMVSAVE ELHEAFGLAE EAAAVRS
