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Database: UniProt
Entry: A0A1S8FGY0_9BURK
LinkDB: A0A1S8FGY0_9BURK
Original site: A0A1S8FGY0_9BURK 
ID   A0A1S8FGY0_9BURK        Unreviewed;       413 AA.
AC   A0A1S8FGY0;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {ECO:0000256|HAMAP-Rule:MF_01106};
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106};
DE              EC=2.3.1.35 {ECO:0000256|HAMAP-Rule:MF_01106};
DE     AltName: Full=Ornithine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106};
DE              Short=OATase {ECO:0000256|HAMAP-Rule:MF_01106};
DE     AltName: Full=Ornithine transacetylase {ECO:0000256|HAMAP-Rule:MF_01106};
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase {ECO:0000256|HAMAP-Rule:MF_01106};
DE              EC=2.3.1.1 {ECO:0000256|HAMAP-Rule:MF_01106};
DE     AltName: Full=N-acetylglutamate synthase {ECO:0000256|HAMAP-Rule:MF_01106};
DE              Short=AGSase {ECO:0000256|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000256|HAMAP-Rule:MF_01106};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000256|HAMAP-Rule:MF_01106};
GN   Name=argJ {ECO:0000256|HAMAP-Rule:MF_01106};
GN   ORFNames=B0B52_12740 {ECO:0000313|EMBL:OOG41197.1};
OS   Polaromonas sp. A23.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=1944133 {ECO:0000313|EMBL:OOG41197.1, ECO:0000313|Proteomes:UP000218978};
RN   [1] {ECO:0000313|EMBL:OOG41197.1, ECO:0000313|Proteomes:UP000218978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A23 {ECO:0000313|EMBL:OOG41197.1,
RC   ECO:0000313|Proteomes:UP000218978};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00000498, ECO:0000256|HAMAP-
CC         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:0000256|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:0000256|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:0000256|HAMAP-
CC       Rule:MF_01106}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC       {ECO:0000256|ARBA:ARBA00011475, ECO:0000256|HAMAP-Rule:MF_01106}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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. {ECO:0000256|HAMAP-Rule:MF_01106}.
CC   -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000256|ARBA:ARBA00006774,
CC       ECO:0000256|HAMAP-Rule:MF_01106}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OOG41197.1}.
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DR   EMBL; MUNO01000022; OOG41197.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8FGY0; -.
DR   STRING; 1944133.B0B52_12740; -.
DR   OrthoDB; 9804242at2; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000218978; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
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   CDD; cd02152; OAT; 1.
DR   Gene3D; 3.10.20.340; ArgJ beta chain, C-terminal domain; 1.
DR   Gene3D; 3.60.70.12; L-amino peptidase D-ALA esterase/amidase; 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   NCBIfam; TIGR00120; ArgJ; 1.
DR   PANTHER; PTHR23100; ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ; 1.
DR   PANTHER; PTHR23100:SF0; ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ, MITOCHONDRIAL; 1.
DR   Pfam; PF01960; ArgJ; 1.
DR   SUPFAM; SSF56266; DmpA/ArgJ-like; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW   Rule:MF_01106}; Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP-
KW   Rule:MF_01106}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218978};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01106}.
FT   CHAIN           1..196
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ
FT                   alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT                   /id="PRO_5023308982"
FT   CHAIN           197..413
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT                   chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT                   /id="PRO_5023308983"
FT   ACT_SITE        197
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         284
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         408
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         413
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   SITE            123
FT                   /note="Involved in the stabilization of negative charge on
FT                   the oxyanion by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   SITE            124
FT                   /note="Involved in the stabilization of negative charge on
FT                   the oxyanion by the formation of the oxyanion hole"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   SITE            196..197
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
SQ   SEQUENCE   413 AA;  43455 MW;  68CD9927AC6740AC CRC64;
     MPVNLLATPA DQLYPVPGVR WGIAEAGIRK AGRKDLSVLL LDEGASVGAV FTQNRFCAAP
     VQICREHLAK NAKQGPGIRA MLINTGNANA GTGADGLSRA QASCAALARE LKVAPEQILP
     FSTGVIMEPL PHERIAAGLP AALADAKADN WGKAAEAIMT TDTVAKAFSS RITLGGASVT
     ITGISKGAGM IRPNMATMLG FMATDARVSQ GLMAQLATEL AEGSFNRVTV DGDTSTNDSF
     VVIASNRAKH PEVTSLDSTE GVALRNAMLD IARKLAQAIV RDGEGATKFI TVRVEGGKTG
     AECRQVAYAI AHSPLVKTAF FASDPNLGRI LAAVGYAGIA DLDQTKIDLY LDDVLVAKNG
     GRHPDYVEAD GQRVMKQSEI TVRVLLGRGD AADTVWTCDL SYDYVKINAD YRS
//
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