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Database: UniProt
Entry: A0A1I5KIE1_9SPHN
LinkDB: A0A1I5KIE1_9SPHN
Original site: A0A1I5KIE1_9SPHN 
ID   A0A1I5KIE1_9SPHN        Unreviewed;       426 AA.
AC   A0A1I5KIE1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   08-MAY-2019, entry version 8.
DE   RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE            EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN   ORFNames=SAMN04488060_0228 {ECO:0000313|EMBL:SFO84426.1};
OS   Erythrobacter nanhaisediminis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter.
OX   NCBI_TaxID=604088 {ECO:0000313|EMBL:SFO84426.1, ECO:0000313|Proteomes:UP000199331};
RN   [1] {ECO:0000313|EMBL:SFO84426.1, ECO:0000313|Proteomes:UP000199331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7715 {ECO:0000313|EMBL:SFO84426.1,
RC   ECO:0000313|Proteomes:UP000199331};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOWZ01000001; SFO84426.1; -; Genomic_DNA.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000199331; 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; 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:UP000199331};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:SFO84426.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Transferase {ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN      280    364       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   426 AA;  45340 MW;  D28B2AC718711E77 CRC64;
     MARIVMKFGG TSMAGTERIR RVANLVRKQA AGGNQVAVVV SAMAGETDRL VNFCREANPL
     YDPAEYDVVV ASGEQVTSGL LALTLQSLGA DARSWLGWQL PVRTVEAHAK ARVEAIDADA
     LTSAMEAGQI AVIPGFQGVS EDGRITTMGR GGSDTSAVAI AAAVKADRCD IYTDVDGVYT
     TDPRIVAKAR KLKAVTYEEM LELASVGAKV LQTRSVGLAM KEGVRVQVLS SFVGDDAIPA
     DELPGTMIVS EEEMNILVEK GEMERQHVTG IAHDKNEAKI ILTRVPDKPG AVAHIFDPLA
     KAAINVDMII QNVGRDKGET DVTFTVPQAD LARAQALLED KRDDIGFNRL ITDSKIAKIS
     VVGVGMKSHA GVASTMFKAL ADRGINIQAI TTSEIKVSVL IDEDETELAV RVLHTAYGLD
     ADDEAA
//
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