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Database: UniProt
Entry: A6FXW8_9DELT
LinkDB: A6FXW8_9DELT
Original site: A6FXW8_9DELT 
ID   A6FXW8_9DELT            Unreviewed;       431 AA.
AC   A6FXW8;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=PPSIR1_22354 {ECO:0000313|EMBL:EDM81706.1};
OS   Plesiocystis pacifica SIR-1.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Nannocystineae; Nannocystaceae; Plesiocystis.
OX   NCBI_TaxID=391625 {ECO:0000313|EMBL:EDM81706.1, ECO:0000313|Proteomes:UP000005801};
RN   [1] {ECO:0000313|EMBL:EDM81706.1, ECO:0000313|Proteomes:UP000005801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIR-1 {ECO:0000313|EMBL:EDM81706.1,
RC   ECO:0000313|Proteomes:UP000005801};
RA   Shimkets L., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) 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:EDM81706.1}.
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DR   EMBL; ABCS01000002; EDM81706.1; -; Genomic_DNA.
DR   RefSeq; WP_006969317.1; NZ_ABCS01000002.1.
DR   STRING; 391625.PPSIR1_22354; -.
DR   EnsemblBacteria; EDM81706; EDM81706; PPSIR1_22354.
DR   eggNOG; ENOG4105CFH; Bacteria.
DR   eggNOG; COG0527; LUCA.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000005801; 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   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF13840; ACT_7; 1.
DR   PIRSF; PIRSF000726; Asp_kin; 2.
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:UP000005801};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:EDM81706.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005801};
KW   Transferase {ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN      287    364       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      370    431       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       6      9       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   NP_BIND     196    197       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   NP_BIND     232    233       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   BINDING      46     46       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000726-1}.
FT   BINDING      97     97       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000726-1}.
FT   BINDING     207    207       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
SQ   SEQUENCE   431 AA;  45290 MW;  9C3C11C5CD4B03F2 CRC64;
     MLVVQKFGGT SVGSLERVRS VAERVLERQR SGDRVVVVVS AMAGETNRLI ALANQLHAIG
     QQAGQATGTD SKGWVAPVKR DDPGFERELS QLVSTGEKVS AALLAMAIQD LGGQAVSLIG
     HQLGLTTSGS FTNARIVSID AANIHRLLDA GSIVVCAGFQ GLDEAGNVTT LGRGGSDTSA
     VALAAAIEAD VCEILTDVDG VFTSDPRIVP TARKLDRISH EEMLELASLG TKVLQIRSVE
     FAKKFNVPVH VRSSLHLGEG TLIVPETPDM EAVLVAGVAL DRDEAKITLT NCPDVPGTIA
     QLFTALGERG IVVDMIIQNA SRAGHTDVTF TVPRAELERA QEAIEALTLE GGEEAGTEVL
     VDPNIAKISI VGVGMRTHAG VAARAFSVLA EEKINIQMVS TSEIKVSVVV DEKYGELALR
     ALHDGFGLGD D
//
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