ID A0A220VCE4_9GAMM Unreviewed; 447 AA.
AC A0A220VCE4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, 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 ORFNames=CF386_02370 {ECO:0000313|EMBL:ASK77970.1};
OS Paraphotobacterium marinum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Paraphotobacterium.
OX NCBI_TaxID=1755811 {ECO:0000313|EMBL:ASK77970.1, ECO:0000313|Proteomes:UP000242175};
RN [1] {ECO:0000313|EMBL:ASK77970.1, ECO:0000313|Proteomes:UP000242175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSCS20N07D {ECO:0000313|EMBL:ASK77970.1,
RC ECO:0000313|Proteomes:UP000242175};
RX PubMed=27154455; DOI=10.1099/ijsem.0.001142;
RA Huang Z., Dong C., Shao Z.;
RT "Paraphotobacterium marinum gen. nov., sp. nov., a member of the family
RT Vibrionaceae, isolated from surface seawater.";
RL Int. J. Syst. Evol. Microbiol. 66:3050-3056(2016).
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}.
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DR EMBL; CP022355; ASK77970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220VCE4; -.
DR KEGG; pmai:CF386_02370; -.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000242175; Chromosome large.
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; cd04912; ACT_AKiii-LysC-EC-like_1; 1.
DR Gene3D; 3.30.70.260; -; 2.
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; IPR002912; ACT_dom.
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 InterPro; IPR018042; Aspartate_kinase_CS.
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; 2.
DR SUPFAM; SSF53633; Carbamate kinase-like; 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, ECO:0000256|PIRSR:PIRSR000726-
KW 1}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU003448};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000726-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242175};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003448}.
FT DOMAIN 313..384
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT BINDING 8..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 221..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000726-1"
SQ SEQUENCE 447 AA; 49172 MW; 1A7BAEC5EF2704E4 CRC64;
MLNLTVAKFG GTSVANYQAM VRSANIVLKN PATKLVVVSA CSGVTNILVQ LSSGKVNEES
SQHLIKKLEN IHTDIIEKIS TTSDLNAKLS EHLNSLKLLV EEINSQYSKI LVDQIVSYGE
VLSSLLFTEI LKELKAQSYC FDVRKVMKTN NSYGQAKPNL ELIKTLTTSH LKPLLTDHIV
VTQGYIGSFG NTTTTLGRGG SDFSAALLAE SCSADVLEIW TDVPGMYTTD PRLTNKARPI
EEISFSEASE MANFGAKILH PSTLIPAIRK NIPVFIGSSI SSNEKGTWIK ESVDSSPLFR
AVTLRKNQTL ITLHSLKMFQ AYGFLAEVFN ILARHKISVD LVTTSEVKIS LTLDNLSTAN
EAPNIPSEAL KELEELCKVE IEQNYSLVAL IGNRISQTNG ANKKVFNALK DYTLRLICYG
ASPHNMCFLV KENVAKEIVN TLHNELF
//
