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Database: UniProt
Entry: F4XTD1_9CYAN
LinkDB: F4XTD1_9CYAN
Original site: F4XTD1_9CYAN 
ID   F4XTD1_9CYAN            Unreviewed;       627 AA.
AC   F4XTD1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=aspartate kinase {ECO:0000256|ARBA:ARBA00013059};
DE            EC=2.7.2.4 {ECO:0000256|ARBA:ARBA00013059};
GN   ORFNames=LYNGBM3L_29060 {ECO:0000313|EMBL:EGJ32167.1};
OS   Moorena producens 3L.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Moorena.
OX   NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ32167.1, ECO:0000313|Proteomes:UP000003959};
RN   [1] {ECO:0000313|Proteomes:UP000003959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX   PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA   Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA   Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA   Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA   Gerwick W.H., Gerwick L.;
RT   "Genomic insights into the physiology and ecology of the marine filamentous
RT   cyanobacterium Lyngbya majuscula.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(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   -!- 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|ARBA:ARBA00004986, ECO:0000256|RuleBase:RU004249}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 1/5. {ECO:0000256|ARBA:ARBA00005139,
CC       ECO:0000256|RuleBase:RU004249}.
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC       {ECO:0000256|ARBA:ARBA00010122}.
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DR   EMBL; GL890928; EGJ32167.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4XTD1; -.
DR   eggNOG; COG0527; Bacteria.
DR   HOGENOM; CLU_009116_3_2_3; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00461.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000003959; 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; cd04261; AAK_AKii-LysC-BS; 1.
DR   CDD; cd04923; ACT_AK-LysC-DapG-like_2; 2.
DR   CDD; cd04913; ACT_AKii-LysC-BS-like_1; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   Gene3D; 3.30.2130.10; VC0802-like; 2.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR041740; AKii-LysC-BS.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR005260; Asp_kin_monofn.
DR   InterPro; IPR001341; Asp_kinase.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   InterPro; IPR027795; CASTOR_ACT_dom.
DR   NCBIfam; TIGR00656; asp_kin_monofn; 1.
DR   NCBIfam; TIGR00657; asp_kinases; 1.
DR   PANTHER; PTHR21499; ASPARTATE KINASE; 1.
DR   PANTHER; PTHR21499:SF3; ASPARTOKINASE; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF13840; ACT_7; 2.
DR   SUPFAM; SSF55021; ACT-like; 3.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   PROSITE; PS51671; ACT; 3.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU004249};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EGJ32167.1};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGJ32167.1}.
FT   DOMAIN          272..351
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   DOMAIN          369..440
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   DOMAIN          462..550
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   627 AA;  66466 MW;  41D8AD2B91A40DC1 CRC64;
     MLIIQKYGGT SVGSVERIKA VAQRVKQTVQ NNNTVVVVVS AMGKTTDDLL SLSKAVSTNP
     SAREMDMLLS TGEQVSIALL SMALQELGQP AISLTGAQVG IITDAEHGRA RILEIQPKRI
     QHYLNQGTVV VVAGFQGMSS GDNFEITTLG RGGSDISAVA LGAALKANLC EIYTDVPGIF
     TTDPRIVPEA QLIPEITCDE MLELASLGAK VLHPRAVEIA RNYGVPLVVR SSWNNAPGTR
     IISPIAKPRS LKGLEINKAV YGVELETNQV KVARWQGRDR LGVVAKLFGE IARDNLDVNL
     IIQSIQEDDA KDIALTVVNR GFEQGETLGA AVSETKLKEL ITSALYGATW QGSEEVEMMV
     EQNMATVAIT GTGMIGRPGV AAKMFSTLAE AGVNIEMIST SELKITCVIN AEVCDRAVAA
     LCQAFEIDRS VVLGPDSIQE FSTDSSPSPV CGAVLDLNQA CITIRHVRDQ PGMAAKLFGQ
     LAQENISVDM IIQSQRCQRL NGIPTCDIAF TVAQADAEAA SMALKALALS IACGEIIVDT
     DIAKVSLVGG GMVAQPLVVA QFFEALAQQQ ITIQMITSSD TKISCVVAQE EGVKALNAVH
     KGSIPVVKNY AQTPKGLATP AKPTYAG
//
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