ID   Q3IHT6_PSET1            Unreviewed;       255 AA.
AC   Q3IHT6;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   02-SEP-2026, entry version 125.
DE   RecName: Full=Acetylglutamate kinase {ECO:0000256|ARBA:ARBA00021197};
DE            EC=2.7.2.8 {ECO:0000256|ARBA:ARBA00013065};
DE   AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000256|ARBA:ARBA00030178};
DE   AltName: Full=NAG kinase {ECO:0000256|ARBA:ARBA00030639};
GN   Name=argB {ECO:0000313|EMBL:CAI87346.1};
GN   OrderedLocusNames=PSHAa2290 {ECO:0000313|EMBL:CAI87346.1};
OS   Pseudoalteromonas translucida (strain TAC 125).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI87346.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI87346.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P., Cheung F.,
RA   Cruveiller S., Damico S., Duilio A., Fang G., Feller G., Mangenot S.,
RA   Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z., Sekowska A.,
RA   Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT   Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-L-glutamate + ATP = N-acetyl-L-glutamyl 5-phosphate +
CC         ADP; Xref=Rhea:RHEA:14629, ChEBI:CHEBI:30616, ChEBI:CHEBI:44337,
CC         ChEBI:CHEBI:57936, ChEBI:CHEBI:456216; EC=2.7.2.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00048141};
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}.
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DR   EMBL; CR954246; CAI87346.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3IHT6; -.
DR   STRING; 326442.PSHAa2290; -.
DR   KEGG; pha:PSHAa2290; -.
DR   eggNOG; COG0548; Bacteria.
DR   HOGENOM; CLU_053680_1_1_6; -.
DR   BioCyc; PHAL326442:PSHA_RS11295-MONOMER; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd04249; AAK_NAGK-NC; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR004662; AcgluKinase_fam.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR041731; NAGK-NC.
DR   NCBIfam; TIGR00761; argB; 1.
DR   PANTHER; PTHR23342; N-ACETYLGLUTAMATE SYNTHASE; 1.
DR   PANTHER; PTHR23342:SF0; N-ACETYLGLUTAMATE SYNTHASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000728; NAGK; 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAI87346.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAI87346.1}.
FT   DOMAIN          4..231
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
SQ   SEQUENCE   255 AA;  27293 MW;  D4B6EE371A2BBAA1 CRC64;
     MSKKTWVIKL GGAVLNTENA AKALFSVLNE QHNAQFVIVH GGGALVDTWL KDAGFASAKH
     QGLRISPKEQ MPYIVGALAG CANKQLMSAA INAGHKPVGL SLYEAGVTAT QKLKALCLVG
     KCTSNDDSII NDLLKIGRMP IVSSIGFDLQ GLWYNVNADE AAAAIANNLN AELIFMTDVE
     AVLDANKQPL HQLDTKHIDT LINEGVIVGG MEVKVKTSLH AAQHLRRGVY ISSWQKPENL
     TALLQGKHVG TKITP
//