(data stored in ACNUC7421 zone)

SWISSPROT: ARGB_PARXL

ID   ARGB_PARXL              Reviewed;         299 AA.
AC   Q146X4;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 81.
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=Bxeno_A0077; ORFNames=Bxe_A4385;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-
CC       L-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;
CC         EC=2.7.2.8; Evidence={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; CP000270; ABE28615.1; -; Genomic_DNA.
DR   RefSeq; WP_007179687.1; NZ_CP008760.1.
DR   SMR; Q146X4; -.
DR   STRING; 266265.Bxe_A4385; -.
DR   EnsemblBacteria; ABE28615; ABE28615; Bxe_A4385.
DR   GeneID; 4005520; -.
DR   KEGG; bxb:DR64_2061; -.
DR   KEGG; bxe:Bxe_A4385; -.
DR   eggNOG; ENOG4105CAS; Bacteria.
DR   eggNOG; COG0548; LUCA.
DR   HOGENOM; HOG000233259; -.
DR   KO; K00930; -.
DR   OMA; PKTECCI; -.
DR   OrthoDB; 901370at2; -.
DR   BioCyc; BXEN266265:BXE_RS00385-MONOMER; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000001817; Chromosome 1.
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   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; IPR041727; NAGK-C.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000728; NAGK; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR00761; argB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q146X4.
DR   SWISS-2DPAGE; Q146X4.
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN         1    299       Acetylglutamate kinase.
FT                                /FTId=PRO_0000264690.
FT   REGION       72     73       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00082}.
FT   BINDING      94     94       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00082}.
FT   BINDING     196    196       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00082}.
FT   SITE         37     37       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00082}.
FT   SITE        256    256       Transition state stabilizer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00082}.
SQ   SEQUENCE   299 AA;  32072 MW;  67B0002CB9778CAD CRC64;
     MSELPDLSQI APTLKAEILA EALPYIRQYH GKTVVIKYGG NAMTEERLKQ GFARDVILLK
     LVGINPVIVH GGGPQIDQAL KKIGKQGTFI QGMRVTDEET MEVVEWVLGG EVQQDIVTLI
     NHFGGHAVGL TGKDGGLIHA RKMLMPDRDN PGQYVDIGQV GEVEAINPAV VKALQDDAFI
     PVISPIGFGE DGLSYNINAD LVAGKLAVVL NAEKLVMMTN IPGVMDKEGN LLTDLSAREI
     DGLFADGTIS GGMLPKISSA LDAAKSGVRS VHIIDGRIEH SVLLEILTEQ PFGTMIRSH
//

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