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AK_THETH
ID   AK_THETH                Reviewed;         405 AA.
AC   P61489; P77991; P97151;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Aspartokinase;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartate kinase;
DE            Short=AK;
DE            Short=ASK;
DE   AltName: Full=Threonine-sensitive AK;
DE            Short=ThrA;
GN   Name=ask; Synonyms=askAB;
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, AND NOMENCLATURE.
RC   STRAIN=ATCC 33923 / DSM 674 / AT-62;
RX   PubMed=7773416; DOI=10.1099/13500872-141-5-1211;
RA   Nishiyama M., Kukimoto M., Beppu T., Horiouchi S.;
RT   "An operon encoding aspartokinase and purine phosphoribosyltransferase in
RT   Thermus flavus.";
RL   Microbiology 141:1211-1219(1995).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-7; GLY-9; GLY-10; SER-41;
RP   ALA-42; THR-47; GLU-74; GLY-135; ARG-150; ASP-154; ASP-174 AND ASP-182,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=16232547; DOI=10.1016/s1389-1723(99)80146-7;
RA   Kobashi N., Nishiyama M., Tanokura M.;
RT   "Kinetic and mutation analyses of aspartate kinase from Thermus flavus.";
RL   J. Biosci. Bioeng. 87:739-745(1999).
RN   [3]
RP   ACTIVITY 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).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 245-405 IN COMPLEX WITH SUBSTRATE
RP   ANALOGS, AND SUBUNIT.
RX   PubMed=19490113; DOI=10.1111/j.1742-4658.2009.07030.x;
RA   Yoshida A., Tomita T., Kono H., Fushinobu S., Kuzuyama T., Nishiyama M.;
RT   "Crystal structures of the regulatory subunit of Thr-sensitive aspartate
RT   kinase from Thermus thermophilus.";
RL   FEBS J. 276:3124-3136(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:0000269|PubMed:16232547, ECO:0000269|PubMed:7773416}.
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:16232547, ECO:0000269|PubMed:7773416};
CC   -!- ACTIVITY REGULATION: Inhibited by threonine.
CC       {ECO:0000269|PubMed:15033471, ECO:0000269|PubMed:16232547,
CC       ECO:0000269|PubMed:7773416}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.27 mM for aspartate {ECO:0000269|PubMed:16232547};
CC         KM=0.5 mM for ATP {ECO:0000269|PubMed:16232547};
CC         Note=kcat is 1500 min(-1).;
CC       Temperature dependence:
CC         Thermostable. {ECO:0000269|PubMed:16232547};
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: Heterotetramer consisting of 2 isoforms Alpha (catalytic and
CC       regulation) and of a homodimer of 2 isoforms Beta (regulation and
CC       thermostability). {ECO:0000269|PubMed:15033471,
CC       ECO:0000269|PubMed:19490113}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Alpha; Synonyms=Aspartokinase subunit alpha;
CC         IsoId=P61489-1; Sequence=Displayed;
CC       Name=Beta; Synonyms=Aspartokinase subunit beta;
CC         IsoId=P61489-2; Sequence=VSP_018665;
CC   -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
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DR   EMBL; D37928; BAA07146.1; -; Genomic_DNA.
DR   EMBL; D37928; BAA07147.1; -; Genomic_DNA.
DR   RefSeq; WP_024118988.1; NZ_AP024270.1. [P61489-1]
DR   PDB; 2DT9; X-ray; 2.15 A; A/B=245-405.
DR   PDB; 2ZHO; X-ray; 2.98 A; A/B/C/D/E/F=245-405.
DR   PDBsum; 2DT9; -.
DR   PDBsum; 2ZHO; -.
DR   AlphaFoldDB; P61489; -.
DR   SMR; P61489; -.
DR   PRIDE; P61489; -.
DR   BRENDA; 2.7.2.4; 2305.
DR   SABIO-RK; P61489; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   EvolutionaryTrace; P61489; -.
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   1: Evidence at protein level;
KW   3D-structure; 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_0000002389"
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   BINDING         274..275
FT                   /ligand="substrate"
FT   BINDING         288..290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="substrate"
FT   BINDING         355..356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         369..370
FT                   /ligand="substrate"
FT   BINDING         376..377
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            7
FT                   /note="Contribution to the catalysis"
FT   SITE            74
FT                   /note="Contribution to the catalysis"
FT   VAR_SEQ         1..244
FT                   /note="Missing (in isoform Beta)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018665"
FT   MUTAGEN         7
FT                   /note="K->A: Loss of aspartokinase activity."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         7
FT                   /note="K->M: Loss of aspartokinase activity."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         9
FT                   /note="G->M: Loss of aspartokinase activity."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         10
FT                   /note="G->A: Significant decrease in the catalytic
FT                   efficiency."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         41
FT                   /note="S->A: Significant decrease in the catalytic
FT                   efficiency. Requires higher concentration of magnesium ion
FT                   than wild-type."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         42
FT                   /note="A->S: Loss of aspartokinase activity."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         47
FT                   /note="T->A: Significant decrease in the affinity for
FT                   aspartic acid. Requires higher concentration of magnesium
FT                   ion than wild-type."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         74
FT                   /note="E->A: Loss of aspartokinase activity."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         74
FT                   /note="E->Q: Loss of aspartokinase activity."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         135
FT                   /note="G->A: Very low catalytic efficiency."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         135
FT                   /note="G->S: Loss of aspartokinase activity."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         150
FT                   /note="R->A: Significant decrease in the catalytic
FT                   efficiency."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         154
FT                   /note="D->A: Significant decrease in the catalytic
FT                   efficiency. Requires higher concentration of magnesium ion
FT                   than wild-type."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         154
FT                   /note="D->N: Significant decrease in the catalytic
FT                   efficiency. Requires higher concentration of magnesium ion
FT                   than wild-type."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         174
FT                   /note="D->A: Significant decrease in the catalytic
FT                   efficiency."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   MUTAGEN         182
FT                   /note="D->A: Significant decrease in the catalytic
FT                   efficiency.Requires higher concentration of magnesium ion
FT                   than wild-type."
FT                   /evidence="ECO:0000269|PubMed:16232547"
FT   STRAND          251..257
FT                   /evidence="ECO:0007829|PDB:2DT9"
FT   STRAND          259..269
FT                   /evidence="ECO:0007829|PDB:2DT9"
FT   HELIX           274..285
FT                   /evidence="ECO:0007829|PDB:2DT9"
FT   STRAND          292..294
FT                   /evidence="ECO:0007829|PDB:2DT9"
FT   STRAND          303..311
FT                   /evidence="ECO:0007829|PDB:2DT9"
FT   HELIX           312..314
FT                   /evidence="ECO:0007829|PDB:2DT9"
FT   HELIX           315..329
FT                   /evidence="ECO:0007829|PDB:2DT9"
FT   STRAND          332..336
FT                   /evidence="ECO:0007829|PDB:2DT9"
FT   STRAND          338..348
FT                   /evidence="ECO:0007829|PDB:2DT9"
FT   HELIX           349..351
FT                   /evidence="ECO:0007829|PDB:2DT9"
FT   HELIX           354..365
FT                   /evidence="ECO:0007829|PDB:2DT9"
FT   STRAND          372..375
FT                   /evidence="ECO:0007829|PDB:2DT9"
FT   STRAND          377..385
FT                   /evidence="ECO:0007829|PDB:2DT9"
FT   HELIX           386..388
FT                   /evidence="ECO:0007829|PDB:2DT9"
FT   HELIX           389..399
FT                   /evidence="ECO:0007829|PDB:2DT9"
SQ   SEQUENCE   405 AA;  43319 MW;  47A3A29E2B82D0EA CRC64;
     MALVVQKYGG TSVGDLERIH KVAQRIAHYR EKGHRLAVVV SAMGHTTDEL IALAKRVNPR
     PPFRELDLLT TTGEQVSVAL LSMQLWAMGI PAKGFVQHQI GITTDGRYGD ARILEVNPAR
     IREALDQGFV 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
 
 
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