ARGB_DESVH
ID ARGB_DESVH Reviewed; 308 AA.
AC Q72C18;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Acetylglutamate kinase {ECO:0000255|HAMAP-Rule:MF_00082};
DE EC=2.7.2.8 {ECO:0000255|HAMAP-Rule:MF_00082};
DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00082};
DE AltName: Full=NAG kinase {ECO:0000255|HAMAP-Rule:MF_00082};
DE Short=NAGK {ECO:0000255|HAMAP-Rule:MF_00082};
GN Name=argB {ECO:0000255|HAMAP-Rule:MF_00082}; OrderedLocusNames=DVU_1466;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-
CC glutamate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00082};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4. {ECO:0000255|HAMAP-
CC Rule:MF_00082}.
CC -!- INTERACTION:
CC Q72C18; Q72C62: DVU_1422; NbExp=2; IntAct=EBI-10069101, EBI-10069095;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00082}.
CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. ArgB
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00082}.
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DR EMBL; AE017285; AAS95944.1; -; Genomic_DNA.
DR RefSeq; WP_010938759.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_010685.1; NC_002937.3.
DR AlphaFoldDB; Q72C18; -.
DR SMR; Q72C18; -.
DR IntAct; Q72C18; 1.
DR STRING; 882.DVU_1466; -.
DR PaxDb; Q72C18; -.
DR EnsemblBacteria; AAS95944; AAS95944; DVU_1466.
DR KEGG; dvu:DVU_1466; -.
DR PATRIC; fig|882.5.peg.1366; -.
DR eggNOG; COG0548; Bacteria.
DR HOGENOM; CLU_053680_0_0_7; -.
DR OMA; EGLYEDW; -.
DR PhylomeDB; Q72C18; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000002194; Chromosome.
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; -; 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 Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF000728; NAGK; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR TIGRFAMs; TIGR00761; argB; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..308
FT /note="Acetylglutamate kinase"
FT /id="PRO_0000112613"
FT BINDING 67..68
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 32
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
FT SITE 253
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00082"
SQ SEQUENCE 308 AA; 33080 MW; E376C8055359D6E0 CRC64;
MDCVENARLQ SKVLIESLPY LRQFHGETVV IKYGGHAMKD EALKKAFALN VALLKLVGIN
PVIVHGGGPQ IGKMLEQLNI QSHFREGLRV TDDATMDVVE MVLVGKVNKE IVNQMNLAGA
KAVGLSGKDG MLIRARKMEM VISKEAQAPE IIDLGKVGEV MGVNTTLLRS LERDGFVPVI
APVGVDDNGE TYNINADAVA GAVAAALKAK RLLLLTDVAG ILDHDKKLIR SVNMREAVNL
FSDGTLTGGM IPKVKCCLEA LEEGVEKAMI IDGRTENCIL LELLTDKGVG TEIVSDRAAQ
AACNCVLR
