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Database: UniProt
Entry: A0A1E5Q6Y9_9PROT
LinkDB: A0A1E5Q6Y9_9PROT
Original site: A0A1E5Q6Y9_9PROT 
ID   A0A1E5Q6Y9_9PROT        Unreviewed;       407 AA.
AC   A0A1E5Q6Y9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   08-MAY-2019, entry version 14.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=BEN30_11685 {ECO:0000313|EMBL:OEJ66731.1};
OS   Magnetovibrio blakemorei.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetovibrio.
OX   NCBI_TaxID=28181 {ECO:0000313|EMBL:OEJ66731.1, ECO:0000313|Proteomes:UP000095347};
RN   [1] {ECO:0000313|EMBL:OEJ66731.1, ECO:0000313|Proteomes:UP000095347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV-1 {ECO:0000313|EMBL:OEJ66731.1,
RC   ECO:0000313|Proteomes:UP000095347};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) 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:OEJ66731.1}.
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DR   EMBL; MCGG01000029; OEJ66731.1; -; Genomic_DNA.
DR   RefSeq; WP_069958251.1; NZ_MCGG01000029.1.
DR   EnsemblBacteria; OEJ66731; OEJ66731; BEN30_11685.
DR   BioCyc; GCF_001746755:BEN30_RS10255-MONOMER; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000095347; 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;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000095347};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:OEJ66731.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095347};
KW   Transferase {ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN      264    348       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   407 AA;  43582 MW;  28DA003E414B9EC3 CRC64;
     MALIVQKFGG TSVGDVERIQ NVAKRVKREV DAGNQVAVVV SAMSGVTNQL VDYVTSINPL
     YDTREYDVVV SSGEQVTAGL LALALQNLGV TARSWMGWQL PVSTDSAHGK ARILDIDCSE
     VLKRLADGEV AVVPGFQGVG SDKRVTTLGR GGSDTSAVAL AAALKADRCD IYTDVDGVYT
     TDPRIVSKAK KLDKITFEEM LEMASLGAKV LQTRSVEVAM KHGVRLQVRS SFSDDEGTLV
     VDEDEIVEHE LISGIAYSRD EAKITLIGVS DEPGIAAKLF GPLAEASINV DMIVQNVSED
     GKSTDMTFTV TKSDMVRAVE TVRKHTAEVS YKDLLADSNV VKISVIGVGM RSHAGIAQRM
     FQALADKGIN IQVISTSEIK VSVLVAEDYT ELALRALHTA YGLDATD
//
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