ID F0C133_9XANT Unreviewed; 869 AA.
AC F0C133;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=aspartate kinase {ECO:0000256|ARBA:ARBA00013059};
DE EC=2.7.2.4 {ECO:0000256|ARBA:ARBA00013059};
GN ORFNames=XGA_0537 {ECO:0000313|EMBL:EGD20764.1};
OS Xanthomonas hortorum ATCC 19865.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas; Xanthomonas hortorum pv. gardneri.
OX NCBI_TaxID=925777 {ECO:0000313|EMBL:EGD20764.1, ECO:0000313|Proteomes:UP000005023};
RN [1] {ECO:0000313|EMBL:EGD20764.1, ECO:0000313|Proteomes:UP000005023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19865 {ECO:0000313|EMBL:EGD20764.1,
RC ECO:0000313|Proteomes:UP000005023};
RX PubMed=21396108; DOI=10.1186/1471-2164-12-146;
RA Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P.,
RA Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., Preston J.F.,
RA Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., Staskawicz B.J.,
RA Jones J.B.;
RT "Comparative genomics reveals diversity among xanthomonads infecting tomato
RT and pepper.";
RL BMC Genomics 12:146-146(2011).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGD20764.1}.
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DR EMBL; AEQX01000051; EGD20764.1; -; Genomic_DNA.
DR RefSeq; WP_006448873.1; NZ_AEQX01000051.1.
DR AlphaFoldDB; F0C133; -.
DR PATRIC; fig|925777.8.peg.5256; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000005023; 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:0008836; F:diaminopimelate decarboxylase activity; IEA:InterPro.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04935; ACT_AKiii-DAPDC_1; 1.
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; IPR018042; Aspartate_kinase_CS.
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; PS00324; ASPARTOKINASE; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGD20764.1};
KW Lyase {ECO:0000313|EMBL:EGD20764.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGD20764.1}.
FT DOMAIN 327..400
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 815
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 538
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 869 AA; 94306 MW; EECA79B5917C9D89 CRC64;
MSAPHTTDRW IVLKFGGTSV SRRHRWDTIG TLASKRANET GGRVLVVVSA LSGVTNELTA
IADGAADSAQ RVAALEQRHR EFLAELELDA DAVLGERLAA LHALLGDARA ATRTLDWQAE
VLGQGELLSS TIGAAYLHAN GLDMGWLDAR QWLSALPPQP NQSEWSKRLS VSCQWQSDAQ
WRSRFDAQPT RLLITQGFIS RHADGGTAIL GRGGSDTSAA YFGALLGASR VEIWTDVPGM
FSANPKEVPD ARLLTRLDYY EAQEIATTGA KVLHPRSIKP CRDSGVPMAI LDTERPDLPG
TSIDGNAEPV LGVKAISRRN GIVLVSMEGI GMWQQVGFLA DVFTLFKKHG LSVDLIGSAE
TNVTVSLDPS ENLVNTDVLA ALSADLSQIC KVKIIVPCAA ITLVGRGMRS LLHKLSDVWA
TFGQERVHMI SQSSNDLNLT FVIDEADADG LLPILHAELI DSGAMPVSEG EVFGPRWREI
IGSVRPRPTP WWHAERAHLL SLSKAGTPRY VYHLPTVRAR AHALAQIAAV DQRYYAIKAN
AHPAILMALE QAGFGLECVS HGELRRVFDT LPELSPRRVL FTPSFAPKAE YEAGFALGVT
VTVDNVEALR RWPEVFRGRN VWLRIDLGHG DGHHEKVNTG GKASKFGLSS TRVDEFVELA
RTLEVTITGV HAHLGSGVET GEHWRMMYDE LAGFARRIGT VETIDIGGGL PIPYSAEDEP
FDLELWAKGL AEVKAVHPGY RLAIEPGRYL VAEAGVLLAQ VTQVIEKDGV QRVGLDAGMN
TLIRPALYDA WHDIENLSQL DAPADGAFDI VGPICESSDV FGKRRRLPAA TAPGDVMLVA
DSGAYGYSMA STYNQRELPR EEVIDAPAG
//
