ARGB_XYLFA
ID ARGB_XYLFA Reviewed; 421 AA.
AC Q9PEM7;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Acetylglutamate kinase;
DE EC=2.7.2.8;
DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase;
DE AltName: Full=NAG kinase;
DE Short=NAGK;
GN Name=argB; OrderedLocusNames=XF_1001;
OS Xylella fastidiosa (strain 9a5c).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=160492;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9a5c;
RX PubMed=10910347; DOI=10.1038/35018003;
RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S.,
RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F.,
RA Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N.,
RA Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F.,
RA Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y.,
RA Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O.,
RA Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R.,
RA Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B.,
RA Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G.,
RA Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M.,
RA da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z.,
RA Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D.,
RA Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S.,
RA Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL Nature 406:151-159(2000).
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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the acetylglutamate
CC kinase family. ArgB subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF83811.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003849; AAF83811.1; ALT_INIT; Genomic_DNA.
DR PIR; H82734; H82734.
DR AlphaFoldDB; Q9PEM7; -.
DR SMR; Q9PEM7; -.
DR STRING; 160492.XF_1001; -.
DR PRIDE; Q9PEM7; -.
DR EnsemblBacteria; AAF83811; AAF83811; XF_1001.
DR KEGG; xfa:XF_1001; -.
DR PATRIC; fig|160492.11.peg.1071; -.
DR eggNOG; COG0548; Bacteria.
DR HOGENOM; CLU_006384_4_1_6; -.
DR OMA; FQTCYHS; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000000812; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04252; AAK_NAGK-fArgBP; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR011242; ArgB_GNAT.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR041734; NAGK-fArgBP.
DR InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF04768; NAT; 1.
DR PIRSF; PIRSF036441; NAGK_DUF619; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR00761; argB; 1.
DR PROSITE; PS51731; GNAT_NAGS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..421
FT /note="Acetylglutamate kinase"
FT /id="PRO_0000112687"
FT DOMAIN 274..420
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..252
FT /note="Acetylglutamate kinase"
FT BINDING 59..60
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 26
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 231
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 421 AA; 46963 MW; 6D4AF549E6392A77 CRC64;
MASTKEISQY LKRFSQLDAK RFAVVKVGGA VLRDDVDALT SSLSFLQEVG LTPIVLHGAG
PQLDEELTAA GIQKKTVNGF RVTLPETMAI VRKVFHTSNL QLIEALQRNG ARATSITGGV
FEAHYLDQET YGLVGEISAV NLAPIEASLR AASIPVIASL GETPSGQILN INADVAANEL
VHVLQPYKII FLTGTGGLLD ADGKIINSIN LSTEYEQLIQ QPWVYGGMKL KIEQIKHLLD
RLPLESSVSI TRPADLAKEL FTHKGSGTLV RRGERVIRAT TWKDLDLPRL QHLIQSSFRR
TLIPHYFETT PLLRAYVSEN YRAAVILTKL GNVPYLDKFA VLDDAQGEGL GRAVWSIMRE
ETPQLFWRSR HNNQANAFYY AESDGYYKQD HWKIFWNGLH HFQQIQQCVA HCAQHPPTLI
D
