ID A0A1D8TNE2_9CYAN Unreviewed; 611 AA.
AC A0A1D8TNE2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=aspartate kinase {ECO:0000256|ARBA:ARBA00013059};
DE EC=2.7.2.4 {ECO:0000256|ARBA:ARBA00013059};
GN ORFNames=BJP34_05185 {ECO:0000313|EMBL:AOW98925.1};
OS Moorena producens PAL-8-15-08-1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Moorena.
OX NCBI_TaxID=1458985 {ECO:0000313|EMBL:AOW98925.1, ECO:0000313|Proteomes:UP000177870};
RN [1] {ECO:0000313|Proteomes:UP000177870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAL-8-15-08-1 {ECO:0000313|Proteomes:UP000177870};
RA Leao T., Castelao G., Korobeynikov A., Monroe E.A., Podell S., Glukhov E.,
RA Allen E., Gerwick W.H., Gerwick L.;
RT "Comparative genomics uncovers the prolific and rare metabolic potential of
RT the cyanobacterial genus Moorea.";
RL Submitted (OCT-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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017599; AOW98925.1; -; Genomic_DNA.
DR RefSeq; WP_070391427.1; NZ_CP017599.1.
DR AlphaFoldDB; A0A1D8TNE2; -.
DR STRING; 1458985.BJP34_05185; -.
DR KEGG; mpro:BJP34_05185; -.
DR OrthoDB; 9799110at2; -.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000177870; Chromosome.
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; 2.
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; 4.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR PROSITE; PS51671; ACT; 4.
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:AOW98925.1};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000177870};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 273..347
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 361..429
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 458..541
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 543..611
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 611 AA; 64682 MW; 5D8D6275F95D5AA1 CRC64;
MALVVQKYGG TSVGSVERIQ AVAQRIIKTV QQDNSVVVVV SAMGKTTDGL VQLAKAISPD
PSRREMDMLL STGEQVSIAL LSMALQELGQ PAISLTGAQV GIVTEAKHSS ARILQIETER
LERSLNEGKV VVVAGFQGIT STDELEITTL GRGGSDTSAV ALAAALGASR CEIYTDVPGI
LTTDPRIVPD AQLMAEITAD EMLELASLGA KVLHPRAVEI ARNYGLTLVV LSSWSDEPGT
RVISPSSPPR SLEGLEIARP VNTVEYDTDQ AKVALLRVPD SPGVAARLFG EIAVQDLDVD
LIIQSIHEQN TNDIAFTVNT NILNRAEAVA EAIAPALRRQ TTPDTQEAEV MVGRDIAKVS
ITGAGMIGRP GVAAQMFQAL ADAGVNIEMI STSEIKVSCV IDALECDRAI AALCNCFDIN
NTPIHLPIRD QAGDSDHSIP VTHPPVRGVA LDIKQARLAI REIPDRPGMA AKIFGTLAEQ
NISIDMIIQS QRCRIINGIA TRDLAFTVPQ AEAEMAQKAL QQIAPVIGCS EILLDADIAK
VSIVGAGMID QPGIAAQMFA ALAEEQINIQ MIATSEIKIS CVVAQDQGVR ALQAIHKAFG
LAGSQKIQVP A
//
