ARGB_XYLFT
ID ARGB_XYLFT Reviewed; 421 AA.
AC Q87EL2;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=PD_0293;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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=AAO28178.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE009442; AAO28178.1; ALT_INIT; Genomic_DNA.
DR PDB; 4NEX; X-ray; 1.70 A; A/B=276-421.
DR PDB; 4NF1; X-ray; 1.40 A; A/B/C/D/E/F/G/H=276-421.
DR PDBsum; 4NEX; -.
DR PDBsum; 4NF1; -.
DR AlphaFoldDB; Q87EL2; -.
DR SMR; Q87EL2; -.
DR EnsemblBacteria; AAO28178; AAO28178; PD_0293.
DR KEGG; xft:PD_0293; -.
DR HOGENOM; CLU_006384_4_1_6; -.
DR OMA; FQTCYHS; -.
DR BRENDA; 2.3.1.1; 6734.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000002516; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Cytoplasm; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..421
FT /note="Acetylglutamate kinase"
FT /id="PRO_0000112688"
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"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:4NEX"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:4NF1"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:4NF1"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:4NF1"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:4NF1"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:4NF1"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:4NF1"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:4NF1"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:4NF1"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:4NF1"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:4NF1"
FT TURN 346..349
FT /evidence="ECO:0007829|PDB:4NF1"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:4NF1"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:4NF1"
FT HELIX 376..382
FT /evidence="ECO:0007829|PDB:4NF1"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:4NF1"
FT STRAND 390..398
FT /evidence="ECO:0007829|PDB:4NF1"
FT HELIX 402..414
FT /evidence="ECO:0007829|PDB:4NF1"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:4NEX"
SQ SEQUENCE 421 AA; 46917 MW; DBD0BF0E2F01AE7C CRC64;
MASAKEISQY LKRFSQLDAK RFAVVKVGGA VLRDDVDALT SSLSFLQEVG LTPIVLHGAG
PQLDEELTAV GIQKKTVNGF RVTLPETMAI VRKVFHATNL QLIEALQRNG ARATSITGGV
FEAHYLDQET YGLVGGISAV NIAPIEASLR AASIPVIASL GETPSGQILN INADVAANEL
VHVLQPYKII FLTGTGGLLD ADGKIINSIN LSTEYEQLIQ QPWVYGGMKL KIEQIKHLLD
RLPLESSVSI TRPADLAKEL FTHKGSGTLI RRGERVIRAT TWKDLDLPRL QHLIQSSFRR
TLIPHYFETT PLLRAYVSEN YRAAVILTKL GNVPYLDKFA VLDDAQGEGL GRAVWSIMRE
ETPQLFWRSR HNNQANAFYY AESDGYYKQD HWKIFWNGLH HFQQIQQCVA HCTQHPPTLI
D
