(data stored in ACNUC7421 zone)

SWISSPROT: ARGB_RHOPS

ID   ARGB_RHOPS              Reviewed;         298 AA.
AC   Q13F27;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   08-MAY-2019, entry version 73.
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=RPD_0072;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE37312.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000283; ABE37312.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011500505.1; NC_007958.1.
DR   SMR; Q13F27; -.
DR   STRING; 316057.RPD_0072; -.
DR   EnsemblBacteria; ABE37312; ABE37312; RPD_0072.
DR   KEGG; rpd:RPD_0072; -.
DR   eggNOG; ENOG4105CAS; Bacteria.
DR   eggNOG; COG0548; LUCA.
DR   HOGENOM; HOG000233259; -.
DR   KO; K00930; -.
DR   OrthoDB; 901370at2; -.
DR   BioCyc; RPAL316057:RPD_RS00360-MONOMER; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000001818; 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   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; Q13F27.
DR   SWISS-2DPAGE; Q13F27.
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN         1    298       Acetylglutamate kinase.
FT                                /FTId=PRO_0000264748.
FT   REGION       69     70       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00082}.
FT   BINDING      91     91       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00082}.
FT   BINDING     196    196       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00082}.
FT   SITE         34     34       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   298 AA;  31416 MW;  17CE65C23FE58DED CRC64;
     MTDAPVISPI DQARILSEAL PHMQRYDEET IVIKYGGHAM GAENDAKAFA RDIVLLEQTA
     VNPVVVHGGG PQIATMLKRL GIKSEFAAGL RITDGATIEI VEMVLAGSIN KQLVGYINEA
     GGKAVGLCGK DGNMVTASKA TRTMVDPDSR IEEVVDLGFV GEPEKVDLTL LNQLIGHELI
     PVLAPLATSA TGQTFNVNAD TFAGAVAGAL KAKRLLLLTD VPGVLDKSKQ LIPELSIKDA
     RKLIADGTIS GGMIPKVETC IYALEQGVEG VVILDGKVPH AVLLELFTNQ GTGTLIHK
//

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