ID A0A2Z6EYX9_9BURK Unreviewed; 299 AA.
AC A0A2Z6EYX9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ECO:0000313|EMBL:GLR01797.1};
GN ORFNames=GCM10007934_16090 {ECO:0000313|EMBL:GLR01797.1}, MCB1EB_2274
GN {ECO:0000313|EMBL:BBE10435.1};
OS Mycoavidus cysteinexigens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Mycoavidus.
OX NCBI_TaxID=1553431 {ECO:0000313|EMBL:BBE10435.1, ECO:0000313|Proteomes:UP000282597};
RN [1] {ECO:0000313|EMBL:BBE10435.1, ECO:0000313|Proteomes:UP000282597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B1-EB {ECO:0000313|EMBL:BBE10435.1,
RC ECO:0000313|Proteomes:UP000282597};
RX PubMed=29540638; DOI=10.1264/jsme2.ME17138;
RA Sharmin D., Guo Y., Nishizawa T., Ohshima S., Sato Y., Takashima Y.,
RA Narisawa K., Ohta H.;
RT "Comparative Genomic Insights into Endofungal Lifestyles of Two Bacterial
RT Endosymbionts, Mycoavidus cysteinexigens and Burkholderia rhizoxinica.";
RL Microbes Environ. 33:66-76(2018).
RN [2] {ECO:0000313|EMBL:GLR01797.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 110909 {ECO:0000313|EMBL:GLR01797.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [3] {ECO:0000313|EMBL:GLR01797.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 110909 {ECO:0000313|EMBL:GLR01797.1};
RA Sun Q., Mori K.;
RT "Draft genome sequence of Mycoavidus cysteinexigens strain NBRC 110909.";
RL Submitted (JAN-2023) 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}.
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DR EMBL; AP018150; BBE10435.1; -; Genomic_DNA.
DR EMBL; BSOD01000032; GLR01797.1; -; Genomic_DNA.
DR RefSeq; WP_045364058.1; NZ_BSOD01000032.1.
DR AlphaFoldDB; A0A2Z6EYX9; -.
DR GeneID; 84624877; -.
DR KEGG; mcys:MCB1EB_2274; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000282597; Chromosome.
DR Proteomes; UP001156688; 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; cd04250; AAK_NAGK-C; 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 InterPro; IPR041727; NAGK-C.
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:BBE10435.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00082};
KW Reference proteome {ECO:0000313|Proteomes:UP000282597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00082}.
FT DOMAIN 32..273
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT BINDING 72..73
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT SITE 37
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT SITE 256
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
SQ SEQUENCE 299 AA; 32049 MW; 597624509DD9F336 CRC64;
MSPKLDLSLI SNELKTHILA EALPHIQRYH GKTVVVKYGG NAMTEQRLKQ GFARDAVLLK
LLGINLVLVH GGGPQIDRAL QKIGKQRVFV QGIRVTDAET MSVVEWVLAG EIQQEIVSLI
NHYGGQAVGL TGKDGGLIRA RQMLAPDQER VGEFLDVGHV GEVEVINPAV IKALLSGAFI
PVISPIGFDD DGASYNLNAD WVASRLATIL NAEKLLIMTN IAGVMDKQGE LLTDLSASQI
DALFADGAIS GGMLPKIRAA LDAAKSGIPA VHIMDGRIEH SLLLEILTEQ SLGTVIRSH
//
