AK_PSEAE
ID AK_PSEAE Reviewed; 412 AA.
AC O69077; Q9I552;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Aspartokinase;
DE EC=2.7.2.4;
DE AltName: Full=Aspartate kinase;
GN Name=lysC; OrderedLocusNames=PA0904;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 198-412.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Hindle Z., Throup J.P., Francis K.P., Bycroft B.W., Williams P.,
RA Stewart G.S.A.B.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-412.
RA Li C., Yang M., Bao R.;
RT "Structural of Pseudomonas aeruginosa Lysc.";
RL Submitted (SEP-2017) to the PDB data bank.
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 -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 1/3.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 1/5.
CC -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}.
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; AE004091; AAG04293.1; -; Genomic_DNA.
DR EMBL; AF061757; AAC16241.1; -; Genomic_DNA.
DR PIR; C83531; C83531.
DR RefSeq; NP_249595.1; NC_002516.2.
DR RefSeq; WP_003085971.1; NZ_QZGE01000007.1.
DR PDB; 5YEI; X-ray; 2.30 A; A/C/E/G=1-412, B/D/F/H=249-412.
DR PDBsum; 5YEI; -.
DR AlphaFoldDB; O69077; -.
DR SMR; O69077; -.
DR STRING; 287.DR97_1039; -.
DR PaxDb; O69077; -.
DR PRIDE; O69077; -.
DR EnsemblBacteria; AAG04293; AAG04293; PA0904.
DR GeneID; 878315; -.
DR KEGG; pae:PA0904; -.
DR PATRIC; fig|208964.12.peg.939; -.
DR PseudoCAP; PA0904; -.
DR HOGENOM; CLU_009116_3_2_6; -.
DR InParanoid; O69077; -.
DR OMA; DMIVQTI; -.
DR PhylomeDB; O69077; -.
DR BioCyc; PAER208964:G1FZ6-920-MON; -.
DR BRENDA; 2.7.2.4; 5087.
DR UniPathway; UPA00034; UER00015.
DR UniPathway; UPA00050; UER00461.
DR UniPathway; UPA00051; UER00462.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004072; F:aspartate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009090; P:homoserine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IBA:GO_Central.
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 Gene3D; 3.40.1160.10; -; 1.
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 Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF13840; ACT_7; 1.
DR PIRSF; PIRSF000726; Asp_kin; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF55021; SSF55021; 2.
DR TIGRFAMs; TIGR00656; asp_kin_monofn; 1.
DR TIGRFAMs; TIGR00657; asp_kinases; 1.
DR PROSITE; PS51671; ACT; 2.
DR PROSITE; PS00324; ASPARTOKINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding;
KW Diaminopimelate biosynthesis; Kinase; Lysine biosynthesis;
KW Nucleotide-binding; Reference proteome; Repeat; Transferase.
FT CHAIN 1..412
FT /note="Aspartokinase"
FT /id="PRO_0000066679"
FT DOMAIN 266..340
FT /note="ACT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT DOMAIN 346..412
FT /note="ACT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:5YEI"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 72..87
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 167..177
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5YEI"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 213..221
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 253..261
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 264..272
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 277..287
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 316..329
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 340..348
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 354..367
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 379..387
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:5YEI"
FT HELIX 391..401
FT /evidence="ECO:0007829|PDB:5YEI"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:5YEI"
SQ SEQUENCE 412 AA; 44389 MW; A06ACAA5E914F337 CRC64;
MALIVQKFGG TSVGTVERIE QVAEKVKKFR EAGDDVVVVV SAMSGETNRL IGLANQIMEQ
PVPRELDVMV STGEQVTIAL LSMALIKRGV PAVSYTGNQV RILTDSAHTK ARILHIDDTH
IRADLKAGRV VVVAGFQGVD GNGNITTLGR GGSDTTGVAL AAALKADECQ IYTDVDGVYT
TDPRVVPQAR RLDKITFEEM LEMASLGSKV LQIRAVEFAG KYNVPLRVLH SFQEGPGTLI
TIDDEEESME QPIISGIAFN RDEAKLTIRG VPDTPGVAFK ILGPISAANV EVDMIVQNVA
HDNTTDFTFT VHRNDYLNAL EILKQTAANI GAREAIGDTN IAKVSIVGVG MRSHAGVASR
MFEALAKESI NIQMISTSEI KVSVVIEEKY LELAVRALHT AFELDAPARQ GE
