ARGB_YERPE
ID ARGB_YERPE Reviewed; 258 AA.
AC Q8ZA87; Q0WA89;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
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=YPO3925, y0311, YP_3124;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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 -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-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=CAL22509.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL22509.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE009952; AAM83902.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS63294.1; -; Genomic_DNA.
DR PIR; AB0478; AB0478.
DR RefSeq; YP_002348799.1; NC_003143.1.
DR PDB; 3T7B; X-ray; 2.50 A; A/B=2-258.
DR PDBsum; 3T7B; -.
DR AlphaFoldDB; Q8ZA87; -.
DR SMR; Q8ZA87; -.
DR STRING; 214092.YPO3925; -.
DR PaxDb; Q8ZA87; -.
DR EnsemblBacteria; AAM83902; AAM83902; y0311.
DR EnsemblBacteria; AAS63294; AAS63294; YP_3124.
DR KEGG; ype:YPO3925; -.
DR KEGG; ypk:y0311; -.
DR KEGG; ypm:YP_3124; -.
DR PATRIC; fig|214092.21.peg.4454; -.
DR eggNOG; COG0548; Bacteria.
DR HOGENOM; CLU_053680_1_1_6; -.
DR OMA; EGLYEDW; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04249; AAK_NAGK-NC; 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; IPR041731; NAGK-NC.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF000728; NAGK; 1.
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..258
FT /note="Acetylglutamate kinase"
FT /id="PRO_0000112689"
FT BINDING 44..45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 181..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 209..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 217
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:3T7B"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:3T7B"
FT HELIX 17..33
FT /evidence="ECO:0007829|PDB:3T7B"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:3T7B"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:3T7B"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:3T7B"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3T7B"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:3T7B"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:3T7B"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:3T7B"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:3T7B"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:3T7B"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:3T7B"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:3T7B"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:3T7B"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:3T7B"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:3T7B"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:3T7B"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:3T7B"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:3T7B"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3T7B"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:3T7B"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:3T7B"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:3T7B"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:3T7B"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:3T7B"
SQ SEQUENCE 258 AA; 26987 MW; B0096A7285B8AA95 CRC64;
MMNPLVIKLG GVLLDSEEAL ERLFTALVTY REKHERPLVI MHGGGCLVDE LMKRLALPVV
KKNGLRVTPA DQIDIITGAL AGTANKTLLA WAVKHQINAV GLCLADGNTV TVTLLDAELG
HVGKAQPGSA ALVQTLLAAG YMPIISSIGI TVEGQLMNVN ADQAATALAA TLGADLILLS
DVSGILDGKG QRIAEMTAQK AEQLIAQGII TDGMVVKVNA ALDAARSLGR PVDIASWRHS
EQLPALFNGV PIGTRISV
