ID G9EM36_9GAMM Unreviewed; 853 AA.
AC G9EM36;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, 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=LDG_6298 {ECO:0000313|EMBL:EHL31636.1};
OS Legionella drancourtii LLAP12.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=658187 {ECO:0000313|EMBL:EHL31636.1, ECO:0000313|Proteomes:UP000002770};
RN [1] {ECO:0000313|EMBL:EHL31636.1, ECO:0000313|Proteomes:UP000002770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LLAP12 {ECO:0000313|EMBL:EHL31636.1,
RC ECO:0000313|Proteomes:UP000002770};
RX PubMed=22047552; DOI=10.1186/1471-2164-12-542;
RA Gimenez G., Bertelli C., Moliner C., Robert C., Raoult D., Fournier P.E.,
RA Greub G.;
RT "Insight into cross-talk between intra-amoebal pathogens.";
RL BMC Genomics 12:542-542(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}.
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DR EMBL; JH413811; EHL31636.1; -; Genomic_DNA.
DR RefSeq; WP_006870233.1; NZ_JH413811.1.
DR AlphaFoldDB; G9EM36; -.
DR STRING; 658187.LDG_6298; -.
DR eggNOG; COG0019; Bacteria.
DR eggNOG; COG0527; Bacteria.
DR HOGENOM; CLU_333395_0_0_6; -.
DR InParanoid; G9EM36; -.
DR OrthoDB; 9802241at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000002770; 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; cd04259; AAK_AK-DapDC; 1.
DR CDD; cd04935; ACT_AKiii-DAPDC_1; 1.
DR CDD; cd04920; ACT_AKiii-DAPDC_2; 1.
DR CDD; cd06840; PLPDE_III_Bif_AspK_DapDC; 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 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; 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; 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.
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:EHL31636.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000002770};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 320..393
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 527
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 853 AA; 94559 MW; 7D1E456B739E8B77 CRC64;
MQQIVTKFGG TSVSTRDTWN NIAAITKKHM STGVQPVIVC SALTQISNKL EKAIEAALIN
EHQSILTDIR NSHLNLAEQL EVNPELIAEE IHQLEQWLTG IALLKQAPAK THAQILSMGE
LMMTRLGHAF LEKQGIHCKW YDARELLTST PFHDGESVNY LSARCESEFD AQLVEKFIAS
GAQAIITQGF FAANPQGETV LLGRGGSDTS AALLAGKLQA AACEIWTDVP GIYTANPHQL
PHARLLKKLN YDEAQEIASM GAKVLHPNCI PPVRRANIPM SVKFTKMPEH SGTLITKDID
ETAPLIKSIQ VKNSILLISI DTLHMWQQVG FLSDVFSAFK HHGFSVDLLS SSEFNVTLSL
DINTKIHDRP AINALLEELN QFGRAKLIEP CSAVSLVGHH IRTVLPQLGP ALEVFDAKQV
YLMSLASNDL NLTFVVDESQ ANQLCQKLHN LLIENNPQIF YYSKSWHEEF GKPAARFTPW
WETERDRLLT TAALNSPCYV YHSPTQAARA QQLLALESID TLFYAIKANP YPSILQTLEK
EGVGFECVSI QELDRILELF PNIDKQRILF TPNFAPKTEY EYALNIGCFI TIDSLYPLEH
WPQLFKNREV IVRIDPGAGA GHHKHVSTAG NESKFGITQN DLAQVIALTK KNNIHVIGLH
AHSGSGILTP ELWQQTASML ASLTEHFPEV KYINLGGGLG IVEKPGQQPL DFANLDALLM
AVKSRYPHLE IWLEPGRFFV AESGVILAKV TQCKEKGKVK FIGIETGMNS LIRPSLYGAY
HEIVNLSRLH EEKAGFSHIV GPICESGDTL GYDRLLPVTE EGDVLLIANA GAYGRCMSSH
YNLRPPAEEI VLD
//
