AK_THET2
ID AK_THET2 Reviewed; 405 AA.
AC P61488; P77991; P97151;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Aspartokinase;
DE EC=2.7.2.4;
DE AltName: Full=Aspartate kinase;
DE Short=ASK;
GN Name=ask; Synonyms=askAB; OrderedLocusNames=TT_C0166;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10074061; DOI=10.1128/jb.181.6.1713-1718.1999;
RA Kobashi N., Nishiyama M., Tanokura M.;
RT "Aspartate kinase-independent lysine synthesis in an extremely thermophilic
RT bacterium, Thermus thermophilus: lysine is synthesized via alpha-
RT aminoadipic acid not via diaminopimelic acid.";
RL J. Bacteriol. 181:1713-1718(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(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 lysine, threonine, isoleucine and
CC methionine. {ECO:0000269|PubMed:10074061}.
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 -!- 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 subunit alpha;
CC IsoId=P61488-1; Sequence=Displayed;
CC Name=Beta; Synonyms=Aspartokinase subunit beta;
CC IsoId=P61488-2; Sequence=VSP_018664;
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show auxotrophy for
CC methionine and threonine. {ECO:0000269|PubMed:10074061}.
CC -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS80514.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB013131; BAA25848.1; -; Genomic_DNA.
DR EMBL; AB013131; BAA25849.1; -; Genomic_DNA.
DR EMBL; AE017221; AAS80514.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011228007.1; NC_005835.1.
DR AlphaFoldDB; P61488; -.
DR SMR; P61488; -.
DR STRING; 262724.TT_C0166; -.
DR EnsemblBacteria; AAS80514; AAS80514; TT_C0166.
DR GeneID; 3168597; -.
DR KEGG; tth:TT_C0166; -.
DR eggNOG; COG0527; Bacteria.
DR HOGENOM; CLU_009116_3_2_0; -.
DR OMA; DMIVQTI; -.
DR OrthoDB; 1067792at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000000592; Chromosome.
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; 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; Repeat; Transferase.
FT CHAIN 1..405
FT /note="Aspartokinase"
FT /id="PRO_0000002387"
FT DOMAIN 263..342
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 344..405
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 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 288..290
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 294
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 74
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_018664"
SQ SEQUENCE 405 AA; 43333 MW; 06F7B79E908960EA CRC64;
MALVVQKYGG TSVGDLERIH KVAQRIAHYR EKGHRLAVVV SAMGHTTDEL IALAKRVNPR
PPFRELDLLT TTGEQVSVAL LSMQLWAMGI PAKGFVQHQI GITTDGRYGD ARILEVNPAR
IREALEQGFV AVIAGFMGTT PEGEITTLGR GGSDTTAVAI AAALGAKECE IYTDTEGVYT
TDPHLIPEAR KLSVIGYDQM LEMAALGARV LHPRAVYYAK RYGVVLHVRS SFSYNPGTLV
KEVAMEMDKA VTGVALDLDH AQIGLIGIPD QPGIAAKVFQ ALAERGIAVD MIIQGVPGHD
PSRQQMAFTV KKDFAQEALE ALEPVLAEIG GEAILRPDIA KVSIVGVGLA STPEVPAKMF
QAVASTGANI EMIATSEVRI SVIIPAEYAE AALRAVHQAF ELDKA
