(data stored in SCRATCH zone)

SWISSPROT: A4F6F7_SACEN

ID   A4F6F7_SACEN            Unreviewed;       421 AA.
AC   A4F6F7;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 95.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   Name=ask {ECO:0000313|EMBL:CAL99631.1};
GN   Synonyms=lysC {ECO:0000313|EMBL:CAL99631.1};
GN   OrderedLocusNames=SACE_0282 {ECO:0000313|EMBL:CAL99631.1};
GN   ORFNames=A8924_0676 {ECO:0000313|EMBL:PFG93434.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99631.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99631.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99631.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93434.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93434.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU003448};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC       {ECO:0000256|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 1/3.
CC       {ECO:0000256|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 1/5. {ECO:0000256|RuleBase:RU004249}.
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC       {ECO:0000256|RuleBase:RU003448}.
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DR   EMBL; AM420293; CAL99631.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93434.1; -; Genomic_DNA.
DR   RefSeq; WP_009946971.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0282; -.
DR   EnsemblBacteria; CAL99631; CAL99631; SACE_0282.
DR   KEGG; sen:SACE_0282; -.
DR   eggNOG; ENOG4105CFH; Bacteria.
DR   eggNOG; COG0527; LUCA.
DR   HOGENOM; HOG000293093; -.
DR   KO; K00928; -.
DR   OMA; INIMMIS; -.
DR   OrthoDB; 1067792at2; -.
DR   BioCyc; SERY405948:SACE_RS01380-MONOMER; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
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; 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   InterPro; IPR001057; Glu/AcGlu_kinase.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF13840; ACT_7; 1.
DR   PIRSF; PIRSF000726; Asp_kin; 2.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SUPFAM; SSF53633; SSF53633; 1.
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;
DR   PRODOM; A4F6F7.
DR   SWISS-2DPAGE; A4F6F7.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:CAL99631.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW   Transferase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:CAL99631.1}.
FT   DOMAIN          267..352
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   NP_BIND         7..10
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   NP_BIND         174..175
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   NP_BIND         210..211
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         47
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         74
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         180
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT   BINDING         185
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
SQ   SEQUENCE   421 AA;  44473 MW;  242AA23B61B8C1D8 CRC64;
     MALVVQKYGG SSLESADRIK RVAERIVETR KAGNDVVVVC SAMGDTTDEL LDLAQQVNPA
     PPERELDMLL TAGERISNAL VAMAIEALGA EARSFSGSQA GVITTSAHQN ARIIDVTPGR
     VQEALKQGQV VLVAGFQGVA QDTKDITTLG RGGSDTTAVA VAAAMNADVC EIYTDVDGVY
     TADPRIVSDA KHLDRITYEE MLEMAATGAK VLHLRAVEYA RRYGVPLHVR SSYSPKSGTI
     VSGSVEDLSV EQAMITGVAH DRSEAKVTVR GVPDNPGIAG RIFRVIADAE IDIDMVLQNV
     SGTASGRTDI TFTVARSNGA LAVTELEKIK DELGFDQVVY DDHVGKVSLV GAGMRSHPGV
     TATFCEALSH AGVNIEIINT SEIRISVLIR DTQLEDAVAA LHAAFELGGD EEAVVYAGSG
     R
//

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