ID A0A431UQE4_STEMA Unreviewed; 442 AA. AC A0A431UQE4; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 14-DEC-2022, entry version 10. DE RecName: Full=Acetylglutamate kinase {ECO:0000256|ARBA:ARBA00021197, ECO:0000256|PIRNR:PIRNR036441}; DE EC=2.7.2.8 {ECO:0000256|ARBA:ARBA00013065, ECO:0000256|PIRNR:PIRNR036441}; GN ORFNames=EKL94_00185 {ECO:0000313|EMBL:RTQ92314.1}; OS Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas OS maltophilia). OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group. OX NCBI_TaxID=40324 {ECO:0000313|EMBL:RTQ92314.1, ECO:0000313|Proteomes:UP000271705}; RN [1] {ECO:0000313|EMBL:RTQ92314.1, ECO:0000313|Proteomes:UP000271705} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MDMC339 {ECO:0000313|EMBL:RTQ92314.1, RC ECO:0000313|Proteomes:UP000271705}; RA Kartti S., Manni A., Chemao El Fihri M.W., Laamarti M., Temsamani L., RA El Jamali J.E., Ouadghiri M., Ibrahimi A., Filati-Maltouf A.; RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases. 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; EC=2.7.2.8; CC Evidence={ECO:0000256|ARBA:ARBA00001679, CC ECO:0000256|PIRNR:PIRNR036441}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl- CC L-ornithine from L-glutamate: step 2/4. CC {ECO:0000256|ARBA:ARBA00004828}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR036441}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RTQ92314.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; RXLZ01000001; RTQ92314.1; -; Genomic_DNA. DR AlphaFoldDB; A0A431UQE4; -. DR UniPathway; UPA00068; UER00107. DR Proteomes; UP000271705; Unassembled WGS sequence. 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-UniRule. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd04252; AAK_NAGK-fArgBP; 1. DR Gene3D; 3.40.1160.10; -; 1. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR004662; AcgluKinase_fam. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR011242; ArgB_GNAT. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR041734; NAGK-fArgBP. DR InterPro; IPR006855; Vertebrate-like_GNAT_dom. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF04768; NAT; 1. DR PIRSF; PIRSF036441; NAGK_DUF619; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR SUPFAM; SSF53633; Carbamate kinase-like; 1. DR TIGRFAMs; TIGR00761; argB; 1. DR PROSITE; PS51731; GNAT_NAGS; 1. PE 4: Predicted; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, KW ECO:0000256|PIRNR:PIRNR036441}; KW Arginine biosynthesis {ECO:0000256|PIRNR:PIRNR036441}; KW ATP-binding {ECO:0000256|PIRNR:PIRNR036441}; KW Cytoplasm {ECO:0000256|PIRNR:PIRNR036441}; KW Kinase {ECO:0000256|PIRNR:PIRNR036441, ECO:0000313|EMBL:RTQ92314.1}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR036441}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036441}. FT DOMAIN 295..441 FT /note="N-acetyltransferase" FT /evidence="ECO:0000259|PROSITE:PS51731" FT BINDING 80..81 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036441-50" FT BINDING 102 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036441-50" FT BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR036441-50" FT SITE 47 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR036441-51" FT SITE 252 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR036441-51" SQ SEQUENCE 442 AA; 48778 MW; E8ECD2D8BC4E7465 CRC64; MSPALQPHRQ TRQTIVRLLS SMASAKEISQ YLKRFSQLDA KRFAVVKVGG AVLRDDLDAL TSSLSFLQEV GLTPIVLHGA GPQLDAELSA AGIEKQTVNG LRVTSPEALA IVRRVFQQSN LRLVEALQQN GARATSITGG VFEAEYLDVD TYGLVGEVKK VNLAPIEASL RAGSIPVITS LGETAGGQIL NVNADFAANE LVQELQPYKI IFLTGTGGLL DEQGNVIDSI NLSTEYDHLI AQPWIHGGMK VKIEQIKDLL DRLPLESSVS ITRPADLAKE LFTHKGSGTL VRKGEKVLRA TAWDELDLPR LKGLIESSFG RTLVPDYFQK TKLLRAYVSE NYRTAVILTD EAEGVYLDKF AVLDDAQGEG LGRAVWNVML EETPQLFWRS RHGNPINHFY YAESEGCYKQ DHWKVFWYGA DGIDRIRTYV DHCGVRAPSL EG //