ARGJ_RHOBA
ID ARGJ_RHOBA Reviewed; 410 AA.
AC Q7UUJ7;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {ECO:0000255|HAMAP-Rule:MF_01106};
DE Includes:
DE RecName: Full=Glutamate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE EC=2.3.1.35 {ECO:0000255|HAMAP-Rule:MF_01106};
DE AltName: Full=Ornithine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE Short=OATase {ECO:0000255|HAMAP-Rule:MF_01106};
DE AltName: Full=Ornithine transacetylase {ECO:0000255|HAMAP-Rule:MF_01106};
DE Includes:
DE RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_01106};
DE AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_01106};
DE Short=AGSase {ECO:0000255|HAMAP-Rule:MF_01106};
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000255|HAMAP-Rule:MF_01106};
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000255|HAMAP-Rule:MF_01106};
GN Name=argJ {ECO:0000255|HAMAP-Rule:MF_01106}; OrderedLocusNames=RB3255;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
CC -!- FUNCTION: Catalyzes two activities which are involved in the cyclic
CC version of arginine biosynthesis: the synthesis of N-acetylglutamate
CC from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by
CC transacetylation between N(2)-acetylornithine and glutamate.
CC {ECO:0000255|HAMAP-Rule:MF_01106}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-
CC acetyl-L-glutamate; Xref=Rhea:RHEA:15349, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:46911, ChEBI:CHEBI:57805; EC=2.3.1.35;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01106};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01106};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine
CC and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine
CC (cyclic): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01106}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4. {ECO:0000255|HAMAP-
CC Rule:MF_01106}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC {ECO:0000255|HAMAP-Rule:MF_01106}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01106}.
CC -!- MISCELLANEOUS: Some bacteria possess a monofunctional ArgJ, i.e.
CC capable of catalyzing only the fifth step of the arginine biosynthetic
CC pathway.
CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC Rule:MF_01106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX294138; CAD73082.1; -; Genomic_DNA.
DR RefSeq; NP_865398.1; NC_005027.1.
DR RefSeq; WP_011119260.1; NC_005027.1.
DR AlphaFoldDB; Q7UUJ7; -.
DR SMR; Q7UUJ7; -.
DR STRING; 243090.RB3255; -.
DR EnsemblBacteria; CAD73082; CAD73082; RB3255.
DR KEGG; rba:RB3255; -.
DR PATRIC; fig|243090.15.peg.1498; -.
DR eggNOG; COG1364; Bacteria.
DR HOGENOM; CLU_027172_1_0_0; -.
DR InParanoid; Q7UUJ7; -.
DR OMA; DYVHENS; -.
DR OrthoDB; 1083409at2; -.
DR UniPathway; UPA00068; UER00106.
DR UniPathway; UPA00068; UER00111.
DR Proteomes; UP000001025; 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:0004358; F:glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006592; P:ornithine biosynthetic process; IBA:GO_Central.
DR CDD; cd02152; OAT; 1.
DR Gene3D; 3.10.20.340; -; 1.
DR HAMAP; MF_01106; ArgJ; 1.
DR InterPro; IPR002813; Arg_biosynth_ArgJ.
DR InterPro; IPR016117; ArgJ-like_dom_sf.
DR InterPro; IPR042195; ArgJ_beta_C.
DR PANTHER; PTHR23100; PTHR23100; 1.
DR Pfam; PF01960; ArgJ; 1.
DR SUPFAM; SSF56266; SSF56266; 1.
DR TIGRFAMs; TIGR00120; ArgJ; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW Autocatalytic cleavage; Cytoplasm; Multifunctional enzyme;
KW Reference proteome; Transferase.
FT CHAIN 1..194
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT /id="PRO_0000002225"
FT CHAIN 195..410
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT /id="PRO_0000002226"
FT ACT_SITE 195
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 282
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 405
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT SITE 119
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT SITE 120
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT SITE 194..195
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
SQ SEQUENCE 410 AA; 42470 MW; AF655CEEF1FF3439 CRC64;
MTDTAPQNDP TTSHVLPKGI RFAGVAAGIK ASGKPDVSLI VTDRPSVMAG VYTTNQIVAA
PVVLTRAKTP TSTGRVVLTN SGNANACTGD EGMQNAKTMC DLAAKLADCD SADVMVMSTG
VIGKPLPMEK VRAGIEAAAG KLGDAESDFI ASADAICTTD QFRKTVSETV TIRGQQFRIA
AMCKGAGMIA PNMATMLGVV MTDAPIGPDA AQASLKQIAG RTFNRVSVDG HTSTNDTVML
VCTGMSVSED AKEFNSDELK IWQEAATQVA LKLAKMLVAD GEGAARFFEV RVSGAADDGD
AFVIAKTVAA SPLVKTAITG GDPNWGRIVS AAGYAGPKIE PERTSLVIDG VTVFENGTPL
SIDAAKLSES MKANSEVLAD LTVGDGPGKA SFWASDLTEA YVRFNSLYTT
