ID A0A199XQQ7_9FLAO Unreviewed; 419 AA.
AC A0A199XQQ7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Aspartokinase {ECO:0000256|RuleBase:RU003448};
DE EC=2.7.2.4 {ECO:0000256|RuleBase:RU003448};
GN Name=lysC {ECO:0000313|EMBL:OAZ03581.1};
GN ORFNames=FLB_18570 {ECO:0000313|EMBL:OAZ03581.1};
OS Flavobacterium succinicans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=29536 {ECO:0000313|EMBL:OAZ03581.1, ECO:0000313|Proteomes:UP000093807};
RN [1] {ECO:0000313|EMBL:OAZ03581.1, ECO:0000313|Proteomes:UP000093807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD5b {ECO:0000313|EMBL:OAZ03581.1,
RC ECO:0000313|Proteomes:UP000093807};
RA Poehlein A., Daniel R., Simeonova D.D.;
RT "Draft genome sequence of Flavobacterium succinicans strain DD5b.";
RL Submitted (JUN-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 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|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 aspartokinase family.
CC {ECO:0000256|ARBA:ARBA00010122, ECO:0000256|RuleBase:RU003448}.
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:OAZ03581.1}.
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DR EMBL; JMTM01000053; OAZ03581.1; -; Genomic_DNA.
DR RefSeq; WP_064715660.1; NZ_JMTM01000053.1.
DR AlphaFoldDB; A0A199XQQ7; -.
DR PATRIC; fig|29536.5.peg.1948; -.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000093807; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04243; AAK_AK-HSDH-like; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 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; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR005260; Asp_kin_monofn.
DR InterPro; IPR001341; Asp_kinase.
DR InterPro; IPR042199; AsparK_Bifunc_asparK/hSer_DH.
DR NCBIfam; TIGR00657; asp_kinases; 1.
DR PANTHER; PTHR21499; ASPARTATE KINASE; 1.
DR PANTHER; PTHR21499:SF59; ASPARTOKINASE; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF000726; Asp_kin; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU004249};
KW ATP-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW Kinase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:OAZ03581.1};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000726-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000093807};
KW Transferase {ECO:0000256|RuleBase:RU003448, ECO:0000313|EMBL:OAZ03581.1}.
FT DOMAIN 2..277
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT BINDING 5..8
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 43
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
SQ SEQUENCE 419 AA; 47823 MW; 96461B2709086412 CRC64;
MRVFKFGGAS VKDAEGIKNV HHVLKTVGYD EVLLVVSAMG KTTNALEEVI KNYFDKSPEL
NSSVQEVKKY HNQIVLDLFE DENHPVFSAV NLLFAELEYF LAHNKSPNYN FVYDQVVSFG
ELISTTILSY FMNFMDIETQ WIDVRNLIKT NANYRDAEVD WEQTKKNITK TIKSKSLNIT
QGFLGSDENN FTTTLGREGS DYTAAIFAYC LNAESVTIWK DVPGVMNADP RYFENASLLN
QISYREAIEL AFYGATVIHP KTLQPLQKKE IPLYVKSFIN PLLKGTSVSK GADLEPQLPC
FIVKRNQLMI SLSSIDFSFI MEENISEIFA LFHQYKIKVN LIQNSAISFS VCVEDKFGNF
GELNAKLSKK FKVEFNEDVT LYTIRHFNDQ AAKLVEENKI VLLKQVSRET MQIITKETL
//
