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Database: UniProt/TrEMBL
Entry: E6T7B2_SHEB6
LinkDB: E6T7B2_SHEB6
Original site: E6T7B2_SHEB6 
ID   E6T7B2_SHEB6            Unreviewed;       260 AA.
AC   E6T7B2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   29-OCT-2014, entry version 26.
DE   RecName: Full=Acetylglutamate kinase {ECO:0000256|HAMAP-Rule:MF_00082};
DE            EC=2.7.2.8 {ECO:0000256|HAMAP-Rule:MF_00082};
DE   AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00082};
DE   AltName: Full=NAG kinase {ECO:0000256|HAMAP-Rule:MF_00082};
GN   Name=argB {ECO:0000256|HAMAP-Rule:MF_00082};
GN   OrderedLocusNames=Sbal678_4245 {ECO:0000313|EMBL:ADT96372.1};
OS   Shewanella baltica (strain OS678).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=693973 {ECO:0000313|EMBL:ADT96372.1, ECO:0000313|Proteomes:UP000007240};
RN   [1] {ECO:0000313|EMBL:ADT96372.1, ECO:0000313|Proteomes:UP000007240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS678 {ECO:0000313|EMBL:ADT96372.1,
RC   ECO:0000313|Proteomes:UP000007240};
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. {ECO:0000256|HAMAP-Rule:MF_00082,
CC       ECO:0000256|SAAS:SAAS00088587}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-L-ornithine from L-glutamate: step 2/4. {ECO:0000256|HAMAP-
CC       Rule:MF_00082, ECO:0000256|SAAS:SAAS00088645}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082}.
CC   -!- SIMILARITY: Belongs to the acetylglutamate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00082}.
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DR   EMBL; CP002383; ADT96372.1; -; Genomic_DNA.
DR   RefSeq; WP_011848138.1; NC_016901.1.
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   OMA; TITSAFQ; -.
DR   BioCyc; SBAL693973:GJDB-4375-MONOMER; -.
DR   UniPathway; UPA00068; UER00107.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-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; SSF53633; 1.
DR   TIGRFAMs; TIGR00761; argB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00088665};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00088593};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00088659};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007240};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00088655};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|SAAS:SAAS00088630};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00082,
KW   ECO:0000256|RuleBase:RU003416}.
FT   REGION       46     47       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00082}.
FT   BINDING      68     68       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00082}.
FT   BINDING     160    160       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00082}.
FT   SITE         11     11       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00082}.
FT   SITE        219    219       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00082}.
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
//
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