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AK_MYCSM
ID   AK_MYCSM                Reviewed;         421 AA.
AC   P41403;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Aspartokinase;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartate kinase;
DE            Short=ASK;
GN   Name=ask;
OS   Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 607 / DSM 43465 / JCM 20379 / NBRC 3207 / NRRL B-692;
RX   PubMed=7910936; DOI=10.1111/j.1365-2958.1994.tb00342.x;
RA   Cirillo J.D., Weisbrod T.R., Pascopella L., Bloom B.R., Jacobs W.R. Jr.;
RT   "Isolation and characterization of the aspartokinase and aspartate
RT   semialdehyde dehydrogenase operon from mycobacteria.";
RL   Mol. Microbiol. 11:629-639(1994).
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: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: Feedback inhibition by lysine and threonine.
CC       {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: Heterotetramer consisting of 2 isoforms Alpha (catalytic and
CC       regulation) and of a homodimer of 2 isoforms Beta (regulation).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Alpha; Synonyms=Aspartokinase subunit alpha;
CC         IsoId=P41403-1; Sequence=Displayed;
CC       Name=Beta; Synonyms=Aspartokinase subunit beta;
CC         IsoId=P41403-2; Sequence=VSP_018662;
CC   -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA78985.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Z17372; CAA78984.1; -; Genomic_DNA.
DR   EMBL; Z17372; CAA78985.1; ALT_INIT; Genomic_DNA.
DR   PIR; S42422; S42422.
DR   RefSeq; WP_003897679.1; NZ_UGQO01000001.1. [P41403-1]
DR   AlphaFoldDB; P41403; -.
DR   SMR; P41403; -.
DR   GeneID; 66737540; -.
DR   OMA; DMIVQTI; -.
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; 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..421
FT                   /note="Aspartokinase"
FT                   /id="PRO_0000002383"
FT   DOMAIN          267..348
FT                   /note="ACT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   DOMAIN          349..421
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         45..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         151..154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         174..175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         180..185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         274..279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         292..294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         360..361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         374..375
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         381..382
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..249
FT                   /note="Missing (in isoform Beta)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_018662"
SQ   SEQUENCE   421 AA;  44458 MW;  926B9FC8625E20CD CRC64;
     MALVVQKYGG SSVADAERIR RVAERIVETK KAGNDVVVVV SAMGDTTDDL LDLARQVSPA
     PPPREMDMLL TAGERISNAL VAMAIESLGA QARSFTGSQA GVITTGTHGN AKIIDVTPGR
     LRDALDEGQI VLVAGFQGVS QDSKDVTTLG RGGSDTTAVA VAAALDADVC EIYTDVDGIF
     TADPRIVPNA RHLDTVSFEE MLEMAACGAK VLMLRCVEYA RRYNVPIHVR SSYSDKPGTI
     VKGSIEDIPM EDAILTGVAH DRSEAKVTVV GLPDVPGYAA KVFRAVAEAD VNIDMVLQNI
     SKIEDGKTDI TFTCARDNGP RAVEKLSALK SEIGFSQVLY DDHIGKVSLI GAGMRSHPGV
     TATFCEALAE AGINIDLIST SEIRISVLIK DTELDKAVSA LHEAFGLGGD DEAVVYAGTG
     R
 
 
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