ID   ARGB_XANAC              Reviewed;         426 AA.
AC   Q8PK29;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-FEB-2003, sequence version 2.
DT   03-AUG-2022, entry version 115.
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=XAC2348;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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=AAM37200.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008923; AAM37200.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8PK29; -.
DR   SMR; Q8PK29; -.
DR   STRING; 190486.XAC2348; -.
DR   EnsemblBacteria; AAM37200; AAM37200; XAC2348.
DR   KEGG; xac:XAC2348; -.
DR   eggNOG; COG0548; Bacteria.
DR   HOGENOM; CLU_006384_4_1_6; -.
DR   OMA; EGLYEDW; -.
DR   UniPathway; UPA00068; UER00107.
DR   Proteomes; UP000000576; 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: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; 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; Transferase.
FT   CHAIN           1..426
FT                   /note="Acetylglutamate kinase"
FT                   /id="PRO_0000112685"
FT   DOMAIN          274..425
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          1..252
FT                   /note="Acetylglutamate kinase"
FT   REGION          253..426
FT                   /note="Unknown"
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   426 AA;  47042 MW;  07C392F8A9FAC93C CRC64;
     MASAKEISQY LKRFSQLDAK RFAVVKVGGA VLRDDLDALT SSLSFLQEVG LTPIVLHGAG
     PQLDAELSAA GIEKHTINGL RVTSPEALAI VRKVFQASNL KLVEALQQNG ARATSITGGV
     FEAEYLDRDI YGLVGEVKAV NLAPIEASLQ AGSIPVITSL GETPSGQILN VNADFAANEL
     VQELQPYKII FLTGTGGLLD ADGKLIDSIN LSTEFDHLMQ QPWINGGMRV KIEQIKDLLD
     RLPLESSVSI TRPSDLAKEL FTHKGSGTLV RRGERVLRAT SWDELDLPRL KSLIESSFGR
     TLVPDYFDTT TLLRAYVSEN YRAAVILTDE GQFGAGRLTY LDKFAVLDDA QGEGLGRAVW
     NVMREETPQL FWRSRHNNQV NIFYYAESDG CIKQEKWKVF WYGLENFEQI QHCVAHCATR
     QPTLLG