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Database: UniProt
Entry: A0A1X0YD54_9DELT
LinkDB: A0A1X0YD54_9DELT
Original site: A0A1X0YD54_9DELT 
ID   A0A1X0YD54_9DELT        Unreviewed;       410 AA.
AC   A0A1X0YD54;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   08-MAY-2019, entry version 9.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=B5V00_03040 {ECO:0000313|EMBL:ORJ63039.1};
OS   Geothermobacter sp. EPR-M.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geothermobacter.
OX   NCBI_TaxID=1969733 {ECO:0000313|EMBL:ORJ63039.1, ECO:0000313|Proteomes:UP000193136};
RN   [1] {ECO:0000313|EMBL:ORJ63039.1, ECO:0000313|Proteomes:UP000193136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPR-M {ECO:0000313|EMBL:ORJ63039.1,
RC   ECO:0000313|Proteomes:UP000193136};
RA   Tully B., Savalia P., Abuyen K., Baughan C., Romero E., Ronkowski C.,
RA   Torres B., Tremblay J., Trujillo A., Tyler M., Perez-Rodriguez I.,
RA   Amend J.;
RT   "Genome sequence of Geothermobacter sp. EPR-M, Deep-Sea Iron
RT   Reducer.";
RL   Submitted (MAR-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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ORJ63039.1}.
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DR   EMBL; NAAD01000002; ORJ63039.1; -; Genomic_DNA.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000193136; 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; 2.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000193136};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:ORJ63039.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193136};
KW   Transferase {ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN      264    338       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      344    410       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       7     10       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   NP_BIND     173    174       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   NP_BIND     209    210       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     179    179       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000726-
FT                                1}.
FT   BINDING     184    184       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
SQ   SEQUENCE   410 AA;  44012 MW;  FA74FC9CB6723B5B CRC64;
     MALVVQKYGG TSVGTVERIR NVARRVAKTY DEGNDVVVIV SAMAGETNRL VALTREICEF
     PNEREYDVVV STGEQVTIGL LAMCLQSMGY AAKSYLGSQI PVRTDAVHAK ARIDSIDDAR
     VRHDLDAGSI IIVAGFQGID PDGNITTLGR GGSDTSAVAM AAALKADVCE IYTDVDGVYT
     TDPRIVDNAS KIEKISYDEM LEMASLGAKV LQIRSVEFAK KYGVVIHVRS SFNDHQGTLV
     TKEDADMETV LVSGIAYNKD EAKISVLGVP DKPGIASQLF TPLAHANITV DMIIQNVSSD
     GITDMTFTVP KGDYRKALQI VGESAREIGA AEVRSDEAIS KISIIGVGMR SHSGVASKMF
     QVLAQEGVNI QMISTSEIKV SCIIDAKYTE LAVRVLHEAF GLGAEDVQQE
//
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