ARGB_CAMJE
ID ARGB_CAMJE Reviewed; 279 AA.
AC Q9PIR8; Q0PBS8; Q9RGZ8;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 136.
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}; OrderedLocusNames=Cj0226;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43431 / TGH 9011 / Serotype O:3;
RX PubMed=10588044; DOI=10.1139/w99-095;
RA Hani E.K., Ng D., Chan V.-L.;
RT "Arginine biosynthesis in Campylobacter jejuni TGH9011: determination of
RT the argCOBD cluster.";
RL Can. J. Microbiol. 45:959-969(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF21804.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAL34381.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF093219; AAF21804.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL111168; CAL34381.1; ALT_INIT; Genomic_DNA.
DR PIR; B81440; B81440.
DR RefSeq; YP_002343669.1; NC_002163.1.
DR AlphaFoldDB; Q9PIR8; -.
DR SMR; Q9PIR8; -.
DR STRING; 192222.Cj0226; -.
DR PaxDb; Q9PIR8; -.
DR PRIDE; Q9PIR8; -.
DR EnsemblBacteria; CAL34381; CAL34381; Cj0226.
DR GeneID; 904554; -.
DR KEGG; cje:Cj0226; -.
DR PATRIC; fig|192222.6.peg.220; -.
DR eggNOG; COG0548; Bacteria.
DR HOGENOM; CLU_053680_0_0_7; -.
DR OMA; EGLYEDW; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000000799; Chromosome.
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: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 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..279
FT /note="Acetylglutamate kinase"
FT /id="PRO_0000112602"
FT BINDING 64..65
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 29
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 238
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT CONFLICT 62
FT /note="H -> R (in Ref. 1; AAF21804)"
FT /evidence="ECO:0000305"
FT CONFLICT 73..76
FT /note="EKLG -> ARLF (in Ref. 1; AAF21804)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="N -> D (in Ref. 1; AAF21804)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="I -> T (in Ref. 1; AAF21804)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="N -> D (in Ref. 1; AAF21804)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="N -> S (in Ref. 1; AAF21804)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 279 AA; 30519 MW; 06770EBBC3E3C96D CRC64;
MQKYLEKANV LIEALPYIRK FNSKIILIKY GGSAMENEEL KHCVMQDIAL LKLVGLKPII
VHGGGKDISA MCEKLGVKSE FKNGLRVSDK ATIEVASMVL NHINKNLVHS LQNLGVKAIG
LCGKDGALLE CVKKDENLAF VGTIQKVNSK ILEELLEKDF LPIIAPIGMD ENFNTYNINA
DDAACAIAKA LRAEKLAFLT DTAGLYEDFN DKNSLISKIS LEQAKILAPK IEGGMHVKLK
SCIDACENGV KKVHILDGRV KHSLLLEFFT DEGIGTLVG
