GenomeNet

Database: UniProt
Entry: A0A2G1QJF6_9RHIZ
LinkDB: A0A2G1QJF6_9RHIZ
Original site: A0A2G1QJF6_9RHIZ 
ID   A0A2G1QJF6_9RHIZ        Unreviewed;       424 AA.
AC   A0A2G1QJF6;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, 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=CSC94_18675 {ECO:0000313|EMBL:PHP65619.1};
OS   Zhengella mangrovi.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Zhengella.
OX   NCBI_TaxID=1982044 {ECO:0000313|EMBL:PHP65619.1, ECO:0000313|Proteomes:UP000221168};
RN   [1] {ECO:0000313|EMBL:PHP65619.1, ECO:0000313|Proteomes:UP000221168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X9-2-2 {ECO:0000313|EMBL:PHP65619.1,
RC   ECO:0000313|Proteomes:UP000221168};
RA   Liao H., Tian Y.;
RT   "Sedimentibacterium mangrovi gen. nov., sp. nov., a novel member of
RT   family Phyllobacteriacea isolated from mangrove sediment.";
RL   Submitted (OCT-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:PHP65619.1}.
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; PDVP01000014; PHP65619.1; -; Genomic_DNA.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000221168; 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:UP000221168};
KW   Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:PHP65619.1};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000221168};
KW   Transferase {ECO:0000256|RuleBase:RU003448}.
FT   DOMAIN      282    357       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      363    424       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND       7     10       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   NP_BIND     180    181       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   NP_BIND     216    217       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
FT   BINDING      47     47       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000726-1}.
FT   BINDING      81     81       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000726-1}.
FT   BINDING     186    186       ATP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000726-
FT                                1}.
FT   BINDING     191    191       ATP. {ECO:0000256|PIRSR:PIRSR000726-1}.
SQ   SEQUENCE   424 AA;  44986 MW;  2B52C25732FF3D20 CRC64;
     MARIVMKFGG TSVADLDRIH NVARHVKREV DAGHEVAVVV SAMAGKTNEL VGWVQAMPKV
     TGAASPFFDA REYDAIVASG EQVTSGLLAI ALQSMGINAR SWQGWQIPVK TDNAHGAARI
     ADIDGSDLIR RFGEGQVAVV AGFQGIGPDN RIATLGRGGS DTSAVAIAAA VKADRCDIYT
     DVDGVYTTDP RIEPKARRLP KVSFEEMLEM ASLGAKVLQV RSVELAMVHK VRTFVRSSFE
     DPDAPGMGDF DNPPGTLICD EDEIVEQQVV TGIAYAKDEA QISLRRVADR PGVSAGIFGP
     LAEANINVDM IVQNISEDGS KTDMTFTVPT GDLDKALAVL DKNRDTVGFD AVQSEGGLVK
     VSVIGIGMRS HAGVAATAFK ALAEKGINIR AITTSEIKIS ILIDGPYAEL AVRTLHSVYG
     LDKA
//
DBGET integrated database retrieval system