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Database: UniProt
Entry: A0A1M3H8Z8_9SPHI
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ID   A0A1M3H8Z8_9SPHI        Unreviewed;       260 AA.
AC   A0A1M3H8Z8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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};
DE            Short=NAGK {ECO:0000256|HAMAP-Rule:MF_00082};
GN   Name=argB {ECO:0000256|HAMAP-Rule:MF_00082};
GN   ORFNames=BGO55_15990 {ECO:0000313|EMBL:OJW54859.1};
OS   Sphingobacteriales bacterium 50-39.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895841 {ECO:0000313|EMBL:OJW54859.1, ECO:0000313|Proteomes:UP000184242};
RN   [1] {ECO:0000313|EMBL:OJW54859.1, ECO:0000313|Proteomes:UP000184242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=50-39 {ECO:0000313|EMBL:OJW54859.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-
CC       glutamate. {ECO:0000256|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; EC=2.7.2.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00001679, ECO:0000256|HAMAP-
CC         Rule:MF_00082};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 2/4. {ECO:0000256|ARBA:ARBA00004828,
CC       ECO:0000256|HAMAP-Rule:MF_00082}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082}.
CC   -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00082}.
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:OJW54859.1}.
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DR   EMBL; MKTZ01000021; OJW54859.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3H8Z8; -.
DR   STRING; 1895841.BGO55_15990; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000184242; Unassembled WGS sequence.
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   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04238; AAK_NAGK-like; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 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   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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00082};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW   Rule:MF_00082}; ATP-binding {ECO:0000256|HAMAP-Rule:MF_00082};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00082};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00082, ECO:0000313|EMBL:OJW54859.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00082};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00082}.
FT   DOMAIN          5..239
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
FT   BINDING         39..40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT   BINDING         61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT   SITE            7
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT   SITE            222
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
SQ   SEQUENCE   260 AA;  27594 MW;  47E188F1F1CC719F CRC64;
     MQLSIIKIGG NIIDDEAKLE LFLDAFAAVK GKKILVHGGG RLATKVATGL GVQQQMIDGR
     RITDAETLKI VTMVYAGTIN KNIVARLQAK GCNAMGLTGA DGNSILAHKR VHPTIDYGFV
     GDVDAVDASL LTSLLMLDKT LVFAPITHDG AGQLLNTNAD TIAQEIARAL CRTFDTSLVY
     SFEKSGVLLD ADDDSTVIGR IDPAYYQELK QKQAIFAGMI PKLDNAFAAL NSGVGKVIIG
     RAEQLPQLLT GASGTTIVHD
//
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