ID E6T7B2_SHEB6 Unreviewed; 260 AA.
AC E6T7B2;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 01-MAY-2013, entry version 18.
DE RecName: Full=Acetylglutamate kinase;
DE EC=2.7.2.8;
DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase;
DE AltName: Full=NAG kinase;
GN Name=argB; OrderedLocusNames=Sbal678_4245;
OS Shewanella baltica (strain OS678).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=693973;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS678;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Konstantinidis K., Deng J.I., Hofle M., Brettar I., Tiedje J.,
RA Auchtung J., Woyke T.;
RT "Complete sequence of chromosome of Shewanella baltica OS678.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-
CC glutamate 5-phosphate.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC acetyl-L-ornithine from L-glutamate: step 2/4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family.
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DR EMBL; CP002383; ADT96372.1; -; Genomic_DNA.
DR RefSeq; YP_005275424.1; NC_016901.1.
DR ProteinModelPortal; E6T7B2; -.
DR EnsemblBacteria; ADT96372; ADT96372; Sbal678_4245.
DR GeneID; 11774198; -.
DR KEGG; sbt:Sbal678_4245; -.
DR KO; K00930; -.
DR UniPathway; UPA00068; UER00107.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:HAMAP.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.1160.10; -; 1.
DR HAMAP; MF_00082_B; ArgB_B; 1; -.
DR InterPro; IPR004662; AcgluKinase.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF000728; NAGK; 1.
DR SUPFAM; SSF53633; Aa_kinase; 1.
DR TIGRFAMs; TIGR00761; argB; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT REGION 46 47 Substrate binding (By similarity).
FT BINDING 68 68 Substrate (By similarity).
FT BINDING 160 160 Substrate (By similarity).
FT SITE 11 11 Transition state stabilizer (By
FT similarity).
FT SITE 219 219 Transition state stabilizer (By
FT similarity).
SQ SEQUENCE 260 AA; 26844 MW; 8BD7335FD7F0607E CRC64;
MSTNNSVLVL KVGGALLQCE MGMARLMDTA AAMLANGQQV LMVHGGGCLV DEQLAANGME
TVKLEGLRVT PPEQMPIIAG ALAGTSNKIL QGAATKAGIV SVGMSLADGN TVSAKIKDER
LGLVGEVTPK DGAYLKFILA QGWMPICSSI AMMDDGQMLN VNADQAATAL AKLVGGKLVL
LSDVSGVLDG KGQLIHSLNG KQIADLVKQG VIEKGMKVKV EAALEVAQWM GQAVQVASWR
DASQLIALAK GEAVGTQIQP
//
