ID A0A0W0R1G6_9GAMM Unreviewed; 854 AA.
AC A0A0W0R1G6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=aspartate kinase {ECO:0000256|ARBA:ARBA00013059};
DE EC=2.7.2.4 {ECO:0000256|ARBA:ARBA00013059};
GN Name=lysAC_2 {ECO:0000313|EMBL:KTC64948.1};
GN Synonyms=lysC_2 {ECO:0000313|EMBL:VEH85631.1};
GN ORFNames=Lade_1755 {ECO:0000313|EMBL:KTC64948.1}, NCTC12735_01266
GN {ECO:0000313|EMBL:VEH85631.1};
OS Legionella adelaidensis.
OG Plasmid 19 {ECO:0000313|EMBL:VEH85631.1,
OG ECO:0000313|Proteomes:UP000281170}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45056 {ECO:0000313|EMBL:KTC64948.1, ECO:0000313|Proteomes:UP000054859};
RN [1] {ECO:0000313|EMBL:KTC64948.1, ECO:0000313|Proteomes:UP000054859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1762-AUS-E {ECO:0000313|EMBL:KTC64948.1,
RC ECO:0000313|Proteomes:UP000054859};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Identification of large and diverse effector repertoires of 38 Legionella
RT species.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:VEH85631.1, ECO:0000313|Proteomes:UP000281170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12735 {ECO:0000313|EMBL:VEH85631.1,
RC ECO:0000313|Proteomes:UP000281170};
RC PLASMID=19 {ECO:0000313|Proteomes:UP000281170};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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; LNKA01000016; KTC64948.1; -; Genomic_DNA.
DR EMBL; LR134428; VEH85631.1; -; Genomic_DNA.
DR RefSeq; WP_058462829.1; NZ_LR134428.1.
DR AlphaFoldDB; A0A0W0R1G6; -.
DR STRING; 45056.Lade_1755; -.
DR KEGG; ladl:NCTC12735_01266; -.
DR PATRIC; fig|45056.6.peg.1812; -.
DR OrthoDB; 9802241at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000054859; Unassembled WGS sequence.
DR Proteomes; UP000281170; Plasmid 19.
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; cd04920; ACT_AKiii-DAPDC_2; 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; IPR002986; DAP_deCOOHase_LysA.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022644; De-COase2_N.
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 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.
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:KTC64948.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Plasmid {ECO:0000313|EMBL:VEH85631.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000054859};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KTC64948.1}.
FT DOMAIN 321..394
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 805
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 854 AA; 94748 MW; 91E4DCF267DB0B09 CRC64;
MRQQLVTKFG GTSVSTRENW KNIAAITKNH LKNGFQPVIV CSALTQASNK LEKLIEAALL
NEHPPLLQEL KEDHFKLADT LEVHHDLIKN ELDQLTQWLT GIALLKQAPA KTRAQILSLG
EIMMTRLGLV FLQNQGINTQ WFDARDALKT TPIDGGDSIN FLAARCTSEP NSQLSSKLAN
CEADAIITQG FIAANKEGET VLLGRGGSDT SAGLLAAILS AHSCEIWTDV PGIYTANPHQ
LPHARLLKQL SYDEAQEIAS MGAKVLHPNC IPPVRRAGIP MVVKYTRLPE HSGTKITYAS
DEYAPPIKSI QVKQNITLIS IDTLNMWQQV GFLADIFNAF RTHGFSVDLL SSSEANVTLS
LDTNAKLRDR AALDALIAEL NTLGRAKIIE PCSAVSLVGH HIRTVLPQLG PTLEVFDAQQ
VYLMSLASND LNLTFVVDEA KADKLCQKLH HLLIENNPQS FYYSKSWQEE FGTPNHRVAP
WWEREKNKLL ALAEMQSPCY IYDLNTQREK AAQLLQLKSI DRLFYALKAN PHPALLNTLY
EKNIGFECVS IFELEHVIAH FPRIEKQKIL FTPNFSGKAE YKFAFSLGCY VTVDNLFPLE
NWPELFQDQS ILIRVDPGCG AGHHRYVCTG GNESKFGIPR QDLLRVASIA KKYNIKIIGL
HAHSGSGILT PELWQETALM LAEEATHFPD VRIINLGGGL GIVEKPGQTP LNLAALDESI
NAVKTRYPHL EFWLEPGRYF VAECGVILAK VTQCKEKGKV KFIGIETGMN SLMRPSLYGS
YHEITNLTRV DEEKTEVAHI VGPICESGDT LGYDRLLPKT GEGDVILIAN TGAYGHCMSS
SYNLRPPAEE IILD
//
