(data stored in ACNUC1104 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   08-MAY-2019, entry version 93.
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.,
RA   Dickens S., 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
CC       novo pathway; L-homoserine from L-aspartate: step 1/3.
CC       {ECO:0000256|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 1/5.
CC       {ECO:0000256|RuleBase:RU004249}.
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC       {ECO:0000256|RuleBase:RU003448}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
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; KNQARVS; -.
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   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
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,
KW   ECO:0000313|EMBL:CAL99631.1}.
FT   DOMAIN      267    352       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       7     10       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   NP_BIND     174    175       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   NP_BIND     210    211       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   BINDING      47     47       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000726-1}.
FT   BINDING      74     74       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000726-1}.
FT   BINDING     180    180       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000726-
FT                                1}.
FT   BINDING     185    185       ATP. {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
//

If you have problems or comments...

PBIL Back to PBIL home page