ID I0IRC7_LEPFC Unreviewed; 404 AA.
AC I0IRC7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
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:BAM07826.1};
GN OrderedLocusNames=LFE_2153 {ECO:0000313|EMBL:BAM07826.1};
OS Leptospirillum ferrooxidans (strain C2-3).
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1162668 {ECO:0000313|EMBL:BAM07826.1, ECO:0000313|Proteomes:UP000007382};
RN [1] {ECO:0000313|EMBL:BAM07826.1, ECO:0000313|Proteomes:UP000007382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2-3 {ECO:0000313|EMBL:BAM07826.1,
RC ECO:0000313|Proteomes:UP000007382};
RX PubMed=22815442; DOI=10.1128/JB.00696-12;
RA Fujimura R., Sato Y., Nishizawa T., Oshima K., Kim S.-W., Hattori M.,
RA Kamijo T., Ohta H.;
RT "Complete Genome Sequence of Leptospirillum ferrooxidans Strain C2-3,
RT Isolated from a Fresh Volcanic Ash Deposit on the Island of Miyake,
RT Japan.";
RL J. Bacteriol. 194:4122-4123(2012).
RN [2] {ECO:0000313|Proteomes:UP000007382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2-3 {ECO:0000313|Proteomes:UP000007382};
RA Fujimura R., Sato Y., Nishizawa T., Nanba K., Oshima K., Hattori M.,
RA Kamijo T., Ohta H.;
RT "The complete genome sequence of the pioneer microbe on fresh volcanic
RT deposit, Leptospirillum ferrooxidans strain C2-3.";
RL Submitted (MAR-2012) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01106}.
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DR EMBL; AP012342; BAM07826.1; -; Genomic_DNA.
DR RefSeq; WP_014450309.1; NC_017094.1.
DR AlphaFoldDB; I0IRC7; -.
DR STRING; 1162668.LFE_2153; -.
DR MEROPS; T05.001; -.
DR GeneID; 78149833; -.
DR KEGG; lfc:LFE_2153; -.
DR PATRIC; fig|1162668.3.peg.2551; -.
DR eggNOG; COG1364; Bacteria.
DR HOGENOM; CLU_027172_1_0_0; -.
DR OrthoDB; 9804242at2; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000007382; 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:UP000007382};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01106}.
FT CHAIN 1..187
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT /id="PRO_5023219610"
FT CHAIN 188..404
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT /id="PRO_5023219609"
FT ACT_SITE 188
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT SITE 114
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 115
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 187..188
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
SQ SEQUENCE 404 AA; 43286 MW; C86996CF278E4BB7 CRC64;
MVKKDRGGVT FPEGFKAAGI HAGIKKKGAL DLGLLVSEKE ALIVGMFTVN KMKAAPVQIS
QRRVRRGIGM AIIVNSGNAN ACTGEQGMAD AMLLTEKVGH YIGCSAQKVL PASTGVIGRN
LPMTSILNAL PALSEKISPK GYVDFSKAIM TTDTYPKSSQ KEVLIGGKIV RIGGSAKGVG
MIHPNMATML VFITTDAVIE KDALRASLHQ IVEEQFHTLS VDGDTSTNDS VYLMANQMAG
NPVIGKGTEW HREFTQALME VASELRNLLL RDAEGATKFL HLVIQGARSK SDAKKIASTI
AKSLLVKTAF YGEDVNWGRI MAAIGNAGVP VRTEKILIAV GDVALVEHGV GLGVDQEEKA
LEVLKKSDIT VTVHLGMGQM TAEYWTTDLS YEYVRINAGY KGRT
//
