ARGB_STRMU
ID ARGB_STRMU Reviewed; 245 AA.
AC Q8DV44;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=SMU_665;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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}.
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DR EMBL; AE014133; AAN58399.1; -; Genomic_DNA.
DR RefSeq; NP_721093.1; NC_004350.2.
DR RefSeq; WP_002261876.1; NC_004350.2.
DR PDB; 3L86; X-ray; 2.06 A; A=1-245.
DR PDBsum; 3L86; -.
DR AlphaFoldDB; Q8DV44; -.
DR SMR; Q8DV44; -.
DR STRING; 210007.SMU_665; -.
DR PRIDE; Q8DV44; -.
DR EnsemblBacteria; AAN58399; AAN58399; SMU_665.
DR KEGG; smu:SMU_665; -.
DR PATRIC; fig|210007.7.peg.590; -.
DR eggNOG; COG0548; Bacteria.
DR HOGENOM; CLU_053680_1_0_9; -.
DR OMA; EGLYEDW; -.
DR PhylomeDB; Q8DV44; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000002512; 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 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 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; Reference proteome; Transferase.
FT CHAIN 1..245
FT /note="Acetylglutamate kinase"
FT /id="PRO_0000112673"
FT BINDING 41..42
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 8
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 215
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:3L86"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:3L86"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:3L86"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:3L86"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:3L86"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:3L86"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:3L86"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:3L86"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:3L86"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:3L86"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:3L86"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:3L86"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:3L86"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:3L86"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:3L86"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:3L86"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:3L86"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:3L86"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3L86"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:3L86"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:3L86"
FT HELIX 212..224
FT /evidence="ECO:0007829|PDB:3L86"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:3L86"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:3L86"
SQ SEQUENCE 245 AA; 26312 MW; D574492F3DEDC613 CRC64;
MKDIIVIKIG GVASQQLSGD FLSQIKNWQD AGKQLVIVHG GGFAINKLME ENQVPVKKIN
GLRVTSKDDM VLVSHALLDL VGKNLQEKLR QAGVSCQQLK SDIKHVVAAD YLDKDTYGYV
GDVTHINKRV IEEFLENRQI PILASLGYSK EGDMLNINAD YLATAVAVAL AADKLILMTN
VKGVLENGAV LEKITSHQVQ EKIDTAVITA GMIPKIESAA KTVAAGVGQV LIGDNLLTGT
LITAD
