GenomeNet

Database: UniProt
Entry: A0A0A8HQE8_STAHY
LinkDB: A0A0A8HQE8_STAHY
Original site: A0A0A8HQE8_STAHY 
ID   A0A0A8HQE8_STAHY        Unreviewed;       449 AA.
AC   A0A0A8HQE8;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   05-JUN-2019, entry version 35.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=SHYC_07760 {ECO:0000313|EMBL:AJC96291.1};
OS   Staphylococcus hyicus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1284 {ECO:0000313|EMBL:AJC96291.1, ECO:0000313|Proteomes:UP000031102};
RN   [1] {ECO:0000313|EMBL:AJC96291.1, ECO:0000313|Proteomes:UP000031102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11249 {ECO:0000313|EMBL:AJC96291.1,
RC   ECO:0000313|Proteomes:UP000031102};
RX   PubMed=25700402;
RA   Calcutt M.J., Foecking M.F., Hsieh H.Y., Adkins P.R., Stewart G.C.,
RA   Middleton J.R.;
RT   "Sequence Analysis of Staphylococcus hyicus ATCC 11249T, an
RT   Etiological Agent of Exudative Epidermitis in Swine, Reveals a Type
RT   VII Secretion System Locus and a Novel 116-Kilobase Genomic Island
RT   Harboring Toxin-Encoding Genes.";
RL   Genome Announc. 3:e01525-14(2015).
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; CP008747; AJC96291.1; -; Genomic_DNA.
DR   RefSeq; WP_039645917.1; NZ_PZHU01000051.1.
DR   EnsemblBacteria; AJC96291; AJC96291; SHYC_07760.
DR   KEGG; shu:SHYC_07760; -.
DR   KO; K00928; -.
DR   OMA; KNQARVS; -.
DR   OrthoDB; 1067792at2; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000031102; Chromosome.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
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; cd04245; AAK_AKiii-YclM-BS; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR035804; AKIII_YclM_N.
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   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01842; ACT; 1.
DR   PIRSF; PIRSF000726; Asp_kin; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00657; asp_kinases; 1.
DR   PROSITE; PS51671; ACT; 2.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031102};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:AJC96291.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031102};
KW   Transferase {ECO:0000256|RuleBase:RU003448,
KW   ECO:0000313|EMBL:AJC96291.1}.
SQ   SEQUENCE   449 AA;  50498 MW;  CC8E2EC64B18B72B CRC64;
     MKVSKFGGSS VATAEQIQKV LNIINSDNER QIVIVSAPGK RHDKDTKTTD LLIRLYEKVI
     NQLDYQHKKS EILERFNDII KGLDLKTNIL EEIDSTLEQL ILELKDEPQR LLDALKSSGE
     NFNAKIIAAY NTEQGVPTEY LSPKEAGIIV TDEPGNAQIL ESSYEKINEL NQRKHKIIIP
     GFFGYSEKGN IVTFPRGGSD ITGAIIARGV RAKLYENFTD VSGIYRANPN VIHDPEIISE
     ITYREMRELS YAGFGVFHDE ALQPLYRYRI PVVIKNTNRP DDPGTYILHD REFNRKKVVL
     GISCDKGFTS INIKKYLMNR QVGFTVKILN ILAENNISFD HMPSGIDNIS IIMRTNQIRG
     KEQKILEAIR KECDIDELNI EQDLAILMVV GEGMSATVGT ANKITTALAD ANINLRMINQ
     GSSEISMMFG ISNNDAELAV KACYDKCYN
//
DBGET integrated database retrieval system