AK_METJA
ID AK_METJA Reviewed; 473 AA.
AC Q57991;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable aspartokinase;
DE EC=2.7.2.4;
DE AltName: Full=Aspartate kinase;
GN OrderedLocusNames=MJ0571;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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 -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
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DR EMBL; L77117; AAB98565.1; -; Genomic_DNA.
DR PIR; C64371; C64371.
DR RefSeq; WP_010870075.1; NC_000909.1.
DR PDB; 2HMF; X-ray; 2.70 A; A/B/C/D=2-470.
DR PDB; 3C1M; X-ray; 2.30 A; A/B/C/D=1-473.
DR PDB; 3C1N; X-ray; 2.72 A; A/B/C/D=1-473.
DR PDB; 3C20; X-ray; 2.70 A; A/B=1-473.
DR PDBsum; 2HMF; -.
DR PDBsum; 3C1M; -.
DR PDBsum; 3C1N; -.
DR PDBsum; 3C20; -.
DR AlphaFoldDB; Q57991; -.
DR SMR; Q57991; -.
DR STRING; 243232.MJ_0571; -.
DR EnsemblBacteria; AAB98565; AAB98565; MJ_0571.
DR GeneID; 1451436; -.
DR KEGG; mja:MJ_0571; -.
DR eggNOG; arCOG00861; Archaea.
DR HOGENOM; CLU_009116_6_0_2; -.
DR InParanoid; Q57991; -.
DR OMA; DMIVQTI; -.
DR OrthoDB; 20371at2157; -.
DR PhylomeDB; Q57991; -.
DR BioCyc; MetaCyc:MON-20452; -.
DR BRENDA; 2.7.2.4; 3260.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR EvolutionaryTrace; Q57991; -.
DR PRO; PR:Q57991; -.
DR Proteomes; UP000000805; 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: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; cd04244; AAK_AK-LysC-like; 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; IPR041746; AK-LysC-like.
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 3D-structure; Amino-acid biosynthesis; ATP-binding; Kinase;
KW Nucleotide-binding; Reference proteome; Repeat; Threonine biosynthesis;
KW Transferase.
FT CHAIN 1..473
FT /note="Probable aspartokinase"
FT /id="PRO_0000066688"
FT DOMAIN 323..392
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 409..473
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3C1M"
FT TURN 9..12
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 45..58
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 62..83
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 87..114
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 119..143
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 187..197
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:3C1M"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 224..234
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:3C1M"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:3C20"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:2HMF"
FT STRAND 311..325
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 331..344
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 370..381
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:3C20"
FT STRAND 395..410
FT /evidence="ECO:0007829|PDB:3C1M"
FT TURN 412..416
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 420..431
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 437..442
FT /evidence="ECO:0007829|PDB:3C1M"
FT STRAND 444..452
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:3C1M"
FT HELIX 456..467
FT /evidence="ECO:0007829|PDB:3C1M"
SQ SEQUENCE 473 AA; 51392 MW; 811C6E0F4B66BC5F CRC64;
MTTVMKFGGT SVGSGERIRH VAKIVTKRKK EDDDVVVVVS AMSEVTNALV EISQQALDVR
DIAKVGDFIK FIREKHYKAI EEAIKSEEIK EEVKKIIDSR IEELEKVLIG VAYLGELTPK
SRDYILSFGE RLSSPILSGA IRDLGEKSIA LEGGEAGIIT DNNFGSARVK RLEVKERLLP
LLKEGIIPVV TGFIGTTEEG YITTLGRGGS DYSAALIGYG LDADIIEIWT DVSGVYTTDP
RLVPTARRIP KLSYIEAMEL AYFGAKVLHP RTIEPAMEKG IPILVKNTFE PESEGTLITN
DMEMSDSIVK AISTIKNVAL INIFGAGMVG VSGTAARIFK ALGEEEVNVI LISQGSSETN
ISLVVSEEDV DKALKALKRE FGDFGKKSFL NNNLIRDVSV DKDVCVISVV GAGMRGAKGI
AGKIFTAVSE SGANIKMIAQ GSSEVNISFV IDEKDLLNCV RKLHEKFIEK TNS
