ARGB_SYNE7
ID ARGB_SYNE7 Reviewed; 301 AA.
AC Q6V1L5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Acetylglutamate kinase {ECO:0000255|HAMAP-Rule:MF_00082};
DE EC=2.7.2.8 {ECO:0000255|HAMAP-Rule:MF_00082};
DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00082};
DE AltName: Full=NAG kinase {ECO:0000255|HAMAP-Rule:MF_00082};
DE Short=NAGK {ECO:0000255|HAMAP-Rule:MF_00082};
GN Name=argB {ECO:0000255|HAMAP-Rule:MF_00082};
GN OrderedLocusNames=Synpcc7942_1496;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15150219; DOI=10.1128/jb.186.11.3346-3354.2004;
RA Burillo S., Luque I., Fuentes I., Contreras A.;
RT "Interactions between the nitrogen signal transduction protein PII and N-
RT acetyl glutamate kinase in organisms that perform oxygenic
RT photosynthesis.";
RL J. Bacteriol. 186:3346-3354(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-
CC glutamate. {ECO:0000255|HAMAP-Rule:MF_00082}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-
CC phosphate; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00082};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4. {ECO:0000255|HAMAP-
CC Rule:MF_00082}.
CC -!- INTERACTION:
CC Q6V1L5; Q6V1L5: argB; NbExp=2; IntAct=EBI-700898, EBI-700898;
CC Q6V1L5; P0A3F4: glnB; NbExp=12; IntAct=EBI-700898, EBI-700889;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00082}.
CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00082}.
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DR EMBL; AY354518; AAQ56594.2; -; Genomic_DNA.
DR EMBL; CP000100; ABB57526.1; -; Genomic_DNA.
DR RefSeq; WP_011244792.1; NC_007604.1.
DR PDB; 2JJ4; X-ray; 3.46 A; A/B/C=1-301.
DR PDB; 2V5H; X-ray; 2.75 A; A/B/C/D/E/F=1-301.
DR PDBsum; 2JJ4; -.
DR PDBsum; 2V5H; -.
DR AlphaFoldDB; Q6V1L5; -.
DR SMR; Q6V1L5; -.
DR DIP; DIP-35009N; -.
DR IntAct; Q6V1L5; 2.
DR STRING; 1140.Synpcc7942_1496; -.
DR PRIDE; Q6V1L5; -.
DR EnsemblBacteria; ABB57526; ABB57526; Synpcc7942_1496.
DR KEGG; syf:Synpcc7942_1496; -.
DR eggNOG; COG0548; Bacteria.
DR HOGENOM; CLU_053680_0_1_3; -.
DR OMA; EGLYEDW; -.
DR OrthoDB; 901370at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1496-MON; -.
DR BRENDA; 2.7.2.8; 7781.
DR UniPathway; UPA00068; UER00107.
DR EvolutionaryTrace; Q6V1L5; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04250; AAK_NAGK-C; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR HAMAP; MF_00082; ArgB; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR037528; ArgB.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR001057; Glu/AcGlu_kinase.
DR InterPro; IPR041727; NAGK-C.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF000728; NAGK; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR SUPFAM; SSF53633; SSF53633; 1.
DR TIGRFAMs; TIGR00761; argB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..301
FT /note="Acetylglutamate kinase"
FT /id="PRO_0000264775"
FT BINDING 70..71
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 35
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 248
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT HELIX 13..19
FT /evidence="ECO:0007829|PDB:2V5H"
FT HELIX 21..26
FT /evidence="ECO:0007829|PDB:2V5H"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2V5H"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:2V5H"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:2V5H"
FT HELIX 44..59
FT /evidence="ECO:0007829|PDB:2V5H"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2V5H"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:2V5H"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2V5H"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:2V5H"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:2V5H"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:2V5H"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:2V5H"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:2V5H"
FT STRAND 145..155
FT /evidence="ECO:0007829|PDB:2V5H"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2V5H"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:2V5H"
FT STRAND 169..177
FT /evidence="ECO:0007829|PDB:2V5H"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2V5H"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:2V5H"
FT STRAND 202..212
FT /evidence="ECO:0007829|PDB:2V5H"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:2V5H"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2V5H"
FT HELIX 229..237
FT /evidence="ECO:0007829|PDB:2V5H"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2JJ4"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:2V5H"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:2V5H"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:2V5H"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:2V5H"
SQ SEQUENCE 301 AA; 32287 MW; 0652E306DEB1947B CRC64;
MSSEFIEAGA ADRVRILSEA LPYLQQFAGR TVVVKYGGAA MKQEELKEAV MRDIVFLACV
GMRPVVVHGG GPEINAWLGR VGIEPQFHNG LRVTDADTME VVEMVLVGRV NKDIVSRINT
TGGRAVGFCG TDGRLVLARP HDQEGIGFVG EVNSVNSEVI EPLLERGYIP VISSVAADEN
GQSFNINADT VAGEIAAALN AEKLILLTDT RGILEDPKRP ESLIPRLNIP QSRELIAQGI
VGGGMIPKVD CCIRSLAQGV RAAHIIDGRI PHALLLEIFT DAGIGTMIVG SGYHEAHQPW
Q
