ID A8IJJ2_AZOC5 Unreviewed; 413 AA.
AC A8IJJ2;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 107.
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 ECO:0000313|EMBL:BAF86312.1};
GN OrderedLocusNames=AZC_0314 {ECO:0000313|EMBL:BAF86312.1};
OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Azorhizobium.
OX NCBI_TaxID=438753 {ECO:0000313|EMBL:BAF86312.1, ECO:0000313|Proteomes:UP000000270};
RN [1] {ECO:0000313|EMBL:BAF86312.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=17720818; DOI=10.1128/AEM.01514-07;
RA Suzuki S., Aono T., Lee KB., Suzuki T., Liu CT., Miwa H., Wakao S., Iki T.,
RA Oyaizu H.;
RT "Rhizobial factors required for stem nodule maturation and maintenance in
RT Sesbania rostrata-Azorhizobium caulinodans ORS571 symbiosis.";
RL Appl. Environ. Microbiol. 73:6650-6659(2007).
RN [2] {ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT caulinodans ORS571.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:BAF86312.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=18522759; DOI=10.1186/1471-2164-9-271;
RA Lee KB., Backer P.D., Aono T., Liu CT., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T.T., Ussery D.W., D'Haeze W., Herder J.D., Gevers D.,
RA Vereecke D., Holsters M., Oyaizu H.;
RT "The genome of the versatile nitrogen fixer Azorhizobium caulinodans
RT ORS571.";
RL BMC Genomics 9:271-271(2008).
RN [4] {ECO:0000313|EMBL:BAF86312.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=19542345; DOI=10.1128/AEM.00398-09;
RA Tsukada S., Aono T., Akiba N., Lee KB., Liu CT., Toyazaki H., Oyaizu H.;
RT "Comparative genome-wide transcriptional profiling of Azorhizobium
RT caulinodans ORS571 grown under free-living and symbiotic conditions.";
RL Appl. Environ. Microbiol. 75:5037-5046(2009).
RN [5] {ECO:0000313|EMBL:BAF86312.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=20382809; DOI=10.1128/AEM.00238-10;
RA Akiba N., Aono T., Toyazaki H., Sato S., Oyaizu H.;
RT "phrR-like gene praR of Azorhizobium caulinodans ORS571 is essential for
RT symbiosis with Sesbania rostrata and is involved in expression of reb
RT genes.";
RL Appl. Environ. Microbiol. 76:3475-3485(2010).
RN [6] {ECO:0000313|EMBL:BAF86312.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=21571889; DOI=10.1128/AEM.02327-10;
RA Liu CT., Lee KB., Wang YS., Peng MH., Lee KT., Suzuki S., Suzuki T.,
RA Oyaizu H.;
RT "Involvement of the azorhizobial chromosome partition gene (parA) in the
RT onset of bacteroid differentiation during Sesbania rostrata stem nodule
RT development.";
RL Appl. Environ. Microbiol. 77:4371-4382(2011).
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}.
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DR EMBL; AP009384; BAF86312.1; -; Genomic_DNA.
DR RefSeq; WP_012168845.1; NC_009937.1.
DR AlphaFoldDB; A8IJJ2; -.
DR STRING; 438753.AZC_0314; -.
DR MEROPS; T05.001; -.
DR KEGG; azc:AZC_0314; -.
DR eggNOG; COG1364; Bacteria.
DR HOGENOM; CLU_027172_1_0_5; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000000270; Chromosome.
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:UP000000270};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01106}.
FT CHAIN 1..194
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT /id="PRO_5023343071"
FT CHAIN 195..413
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT /id="PRO_5023343070"
FT ACT_SITE 195
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 285
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 121
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 122
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 194..195
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
SQ SEQUENCE 413 AA; 42830 MW; AC0F66A75242BB53 CRC64;
MSASISPLAP SALPEVPPVP GVRFATAEAG IRYQGRTDAL LVAFDKGTAV AGVTTRSLCP
SAPVEWCREA LKKGKARGLV VNSGNANAFT GLKGRESTAL TARIAADALG CKPTEIFLAS
TGVIGEPLDA TKFQGVMGDM AGRLAAGPWE GPARAIMTTD TFPKLATAQV PFGNTTVTIA
GIAKGAGMIA PDMATMLSFV FTDAPIAAPV LQKLLSKLVV NSFNAVTVDG DTSTSDTLLL
FATGAAKEVG APAVKDSADP VLRPFRKALK AVLNDLAEQV ARDGEGARKL IRVHVSGAVS
KSSARRIAFS IANSPLVKTA VAGEDANWGR VVMAVGKAGE PADRDRLAIS FGDIRVAAEG
ARDPSYDEQV VSDYMKGDVI DIRVDLGLGK GADRVLTCDL TKEYVAINGD YRS
//
