ARGB_XANCP
ID ARGB_XANCP Reviewed; 426 AA.
AC Q8P8J6;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 118.
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=XCC2245;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
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=AAM41524.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008922; AAM41524.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_637600.1; NC_003902.1.
DR AlphaFoldDB; Q8P8J6; -.
DR SMR; Q8P8J6; -.
DR STRING; 340.xcc-b100_1934; -.
DR EnsemblBacteria; AAM41524; AAM41524; XCC2245.
DR KEGG; xcc:XCC2245; -.
DR PATRIC; fig|190485.4.peg.2395; -.
DR eggNOG; COG0548; Bacteria.
DR HOGENOM; CLU_006384_4_1_6; -.
DR OMA; EGLYEDW; -.
DR BRENDA; 2.7.2.8; 6708.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..426
FT /note="Acetylglutamate kinase"
FT /id="PRO_0000112686"
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; 46953 MW; 12AD709274DA2FB5 CRC64;
MASAKEISQY LKRFSQLDAK RFAVVKVGGA VLRDDLEALT SSLSFLQEVG LTPIVLHGAG
PQLDAELSAA GIEKQTVNGL RVTSPHALAI VRKVFQASNL KLVEALQQNG ARATSITGGV
FEAEYLNRDT YGLVGEVKAV NLAPIEASLQ AGSIPVITSL GETPSGQILN VNADFAANEL
VQELQPYKII FLTGTGGLLD AEGKLIDSIN LSTEYDHLMQ QPWINGGMRV KIEQIKDLLD
RLPLESSVSI TRPADLAKEL FTHKGSGTLV RRGERVLRAT SWDELDLPRL TSLIESSFGR
TLVPDYFSNT KLLRAYVSEN YRAAVILTDE GMLGASALIY LDKFAVLDDA QGEGLGRAVW
NVMREETPQL FWRSRHNNQV NIFYYAESDG CIKQEKWKVF WYGLENFEQI QHCVAHCATR
QPTLLG
