(data stored in ACNUC7421 zone)

SWISSPROT: ARGB_SINFN

ID   ARGB_SINFN              Reviewed;         295 AA.
AC   C3MF41;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   30-AUG-2017, entry version 52.
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=NGR_c00740;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-
CC       L-glutamate. {ECO:0000255|HAMAP-Rule:MF_00082}.
CC   -!- CATALYTIC ACTIVITY: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-
CC       glutamate 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00082}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-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}.
DR   EMBL; CP001389; ACP23878.1; -; Genomic_DNA.
DR   RefSeq; WP_012706663.1; NC_012587.1.
DR   RefSeq; YP_002824631.1; NC_012587.1.
DR   ProteinModelPortal; C3MF41; -.
DR   SMR; C3MF41; -.
DR   STRING; 394.NGR_c00740; -.
DR   EnsemblBacteria; ACP23878; ACP23878; NGR_c00740.
DR   GeneID; 32139487; -.
DR   GeneID; 7790653; -.
DR   KEGG; rhi:NGR_c00740; -.
DR   PATRIC; fig|394.7.peg.2867; -.
DR   eggNOG; ENOG4105CAS; Bacteria.
DR   eggNOG; COG0548; LUCA.
DR   HOGENOM; HOG000233259; -.
DR   KO; K00930; -.
DR   OMA; PKTECCI; -.
DR   OrthoDB; POG091H063W; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00082; ArgB; 1.
DR   InterPro; IPR004662; AcgluKinase.
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   3: Inferred from homology;
DR   PRODOM; C3MF41.
DR   SWISS-2DPAGE; C3MF41.
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN         1    295       Acetylglutamate kinase.
FT                                /FTId=PRO_1000118360.
FT   REGION       66     67       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00082}.
FT   BINDING      88     88       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00082}.
FT   BINDING     193    193       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00082}.
FT   SITE         31     31       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00082}.
FT   SITE        253    253       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00082}.
SQ   SEQUENCE   295 AA;  31221 MW;  9032A7D3B3320594 CRC64;
     MSASESEIQA RLLAQALPYM QRYENKTIVV KYGGHAMGNP ELGRAFASDI ALLKQSGVNP
     IVVHGGGPQI GAMLNKMGIE SKFEGGLRVT DEKTVEIVEM VLAGSINKEI VALINQTGEW
     AIGLCGKDGN MVFAEKARKT IKDPDSNIER ILDLGFVGEV VEVDRTLLDL LARSEMIPVI
     APVAPGRDGH TYNINADTFA GAIAGALNAT RLLFLTDVPG VLDKQGNLIK ELSVAQAHAL
     IADGTISGGM IPKVETCMEA IKAGVQGVVI LNGKTAHSVL LEIFTERGAG TLIVP
//

If you have problems or comments...

PBIL Back to PBIL home page