ID A0A1Q7SUP2_9BACT Unreviewed; 283 AA.
AC A0A1Q7SUP2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=AUF67_14125 {ECO:0000313|EMBL:OLD79932.1};
OS Acidobacteria bacterium 13_1_20CM_58_21.
OC Bacteria; Acidobacteriota.
OX NCBI_TaxID=1803438 {ECO:0000313|EMBL:OLD79932.1, ECO:0000313|Proteomes:UP000186215};
RN [1] {ECO:0000313|EMBL:OLD79932.1, ECO:0000313|Proteomes:UP000186215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLD79932.1}.
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DR EMBL; MNIJ01000205; OLD79932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7SUP2; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000186215; 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:OLD79932.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00082};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00082}.
FT DOMAIN 1..237
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT BINDING 41..42
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT SITE 6
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
FT SITE 219
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00082"
SQ SEQUENCE 283 AA; 29997 MW; 03630423B8506348 CRC64;
MRIVIKFAGA LLEDDATVWS VARQVATLAQ EGHKILVVHG GGRLFTATLK RMAIESKFIA
GLRVTDRETR DVAVMVFAGL LNKKLTAAIS AEGQPAVGVS AADARCFVAE PMVHNEVEGR
LGFVGYLTGL NAQFIESLWR EKLLPVAPCL GLGPNNELYN INADHMAAAC AEYLAADQLI
YLTDVAGVLD GERVLSVVTC EDIERLVQCR VVSGGMVLKL EAAKRAIEGG VREVRIVGGT
SPEALLLSSH AAETSANDRV TSIPGTRVLR VPLAAAQAAL SVA
//