ID A0A0G9H6L6_9GAMM Unreviewed; 853 AA.
AC A0A0G9H6L6;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=aspartate kinase {ECO:0000256|ARBA:ARBA00013059};
DE EC=2.7.2.4 {ECO:0000256|ARBA:ARBA00013059};
GN ORFNames=BJI69_02835 {ECO:0000313|EMBL:APG06316.1}, Y883_19520
GN {ECO:0000313|EMBL:KLD63337.1};
OS Luteibacter rhizovicinus DSM 16549.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Luteibacter.
OX NCBI_TaxID=1440763 {ECO:0000313|EMBL:APG06316.1, ECO:0000313|Proteomes:UP000182987};
RN [1] {ECO:0000313|EMBL:KLD63337.1, ECO:0000313|Proteomes:UP000035585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16549 {ECO:0000313|EMBL:KLD63337.1,
RC ECO:0000313|Proteomes:UP000035585};
RX PubMed=25481407; DOI=10.1007/s10482-014-0344-8;
RA Naushad S., Adeolu M., Wong S., Sohail M., Schellhorn H.E., Gupta R.S.;
RT "A phylogenomic and molecular marker based taxonomic framework for the
RT order Xanthomonadales: proposal to transfer the families Algiphilaceae and
RT Solimonadaceae to the order Nevskiales ord. nov. and to create a new family
RT within the order Xanthomonadales, the family Rhodanobacteraceae fam. nov.,
RT containing the genus Rhodanobacter and its closest relatives.";
RL Antonie Van Leeuwenhoek 107:467-485(2015).
RN [2] {ECO:0000313|EMBL:APG06316.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LJ96 {ECO:0000313|EMBL:APG06316.1};
RX PubMed=28123952;
RA Aamot H.U., Hofgaard I.S., Lysoe E.;
RT "Complete genome sequence of Luteibacter rhizovicinus strain LJ96T,
RT isolated from the rhizosphere of barley (Hordeum vulgare L.) in Denmark.";
RL Genom Data 11:104-105(2016).
RN [3] {ECO:0000313|Proteomes:UP000182987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LJ96T {ECO:0000313|Proteomes:UP000182987};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-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|ARBA:ARBA00000709};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600183-50};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004766, ECO:0000256|RuleBase:RU004249}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 1/3.
CC {ECO:0000256|RuleBase:RU004249}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5. {ECO:0000256|RuleBase:RU004249}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000256|RuleBase:RU003737}.
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DR EMBL; CP017480; APG06316.1; -; Genomic_DNA.
DR EMBL; JPLB01000079; KLD63337.1; -; Genomic_DNA.
DR RefSeq; WP_046969489.1; NZ_CP017480.1.
DR AlphaFoldDB; A0A0G9H6L6; -.
DR STRING; 1440763.BJI69_02835; -.
DR KEGG; lrz:BJI69_02835; -.
DR PATRIC; fig|1440763.5.peg.4079; -.
DR OrthoDB; 9802241at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000035585; Unassembled WGS sequence.
DR Proteomes; UP000182987; Chromosome.
DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:InterPro.
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 Gene3D; 3.30.70.260; -; 2.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR Gene3D; 1.20.120.1320; Aspartokinase, catalytic domain; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR042199; AsparK_Bifunc_asparK/hSer_DH.
DR InterPro; IPR011246; DAP_dec_asp_kin.
DR InterPro; IPR002986; DAP_deCOOHase_LysA.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022657; De-COase2_CS.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR00657; asp_kinases; 1.
DR NCBIfam; TIGR01048; lysA; 1.
DR PANTHER; PTHR43727; DIAMINOPIMELATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43727:SF2; DIAMINOPIMELATE DECARBOXYLASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR PIRSF; PIRSF036459; DAP_dec_asp_kin; 1.
DR PRINTS; PR01181; DAPDCRBXLASE.
DR PRINTS; PR01179; ODADCRBXLASE.
DR SUPFAM; SSF55021; ACT-like; 2.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW Kinase {ECO:0000313|EMBL:KLD63337.1}; Lyase {ECO:0000313|EMBL:KLD63337.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Transferase {ECO:0000313|EMBL:KLD63337.1}.
FT DOMAIN 315..388
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 804
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 528
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 853 AA; 91649 MW; A44365B718E27304 CRC64;
MKFGGTSVAT AARWRNILEL AASRRAEGAR VLIVVSALSG ITDGLKQLCT HADSKRRSDA
AAALADRHHA LLGEMSLAMP DTLGARLSDL SGLAEAGAAE LGELAWQARV QAHGELMSSA
LGAAFLSANG LPTAWLDARE CLHSVALPNQ NERTRLLSAM VEPHHDPALS AALAARGEVF
ITQGFIARDE AGRTVLLGRG GSDTSAAYFG ALLAALRVEI WTDVAGMFSA NPRQVAGARL
LQRLDYEEAQ EIASTGAKVL HPRCLSPLRE PRVPLLIKDT NRPELEGTSI GPEVREHAPS
IKAISARKGI TLVSMESVGM WQQVGFLADV FDAFKRHGLS VDLIGSAETN VTVSLDPTEN
LLDSDAIAAL AADLARVCRV KVIAPCAAIT LVGRGMRSML HKLSGVLAEF GQLRVHLISQ
SSNNLNITFV VDEDVVDDML PRLHELLIGA GALRTDDSMV FGPSWQTLYG AGDPVLPAAA
WWQGERAKLV QLAEERTPRY VYHLPTVRAQ ARRVKSLRAV DRAHYAVKAN THPGILKVLA
EEGFAFECVS PGELAAVSAV VPDDVPLLFT PNFAARRDFE AALRTRATIT IDALHPIEHW
GEMFAGREIM LRVDLGRGLG HHDKVKTGGT GSKFGVPIEH LDRFLRLADL AGARVIGLHA
HLGSGILDAA HWGEVYSQLA SLAERIGTIR VLNIGGGLGV PSHPGETALD MSALDRVLTA
VRQAYPQFDL WMEPGRYLVA DAGVLLAKVT QEKEKGAGMR YLGLDTGMNS LIRPALYDAW
HEITNLSRYG EAATTMYQVV GPICESGDIL GSDRRLPESK EDDVVLVAQG GAYGAAMSSR
YNLRDEADEV LLP
//
