ID L2F644_9GAMM Unreviewed; 400 AA.
AC L2F644;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
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:ELA08251.1};
GN ORFNames=MOMA_06806 {ECO:0000313|EMBL:ELA08251.1};
OS Moraxella macacae 0408225.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=1230338 {ECO:0000313|EMBL:ELA08251.1, ECO:0000313|Proteomes:UP000023795};
RN [1] {ECO:0000313|EMBL:ELA08251.1, ECO:0000313|Proteomes:UP000023795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0408225 {ECO:0000313|EMBL:ELA08251.1,
RC ECO:0000313|Proteomes:UP000023795};
RX PubMed=23409273;
RA Ladner J.T., Whitehouse C.A., Koroleva G.I., Palacios G.F.;
RT "Genome Sequence of Moraxella macacae 0408225, a Novel Bacterial Species
RT Isolated from a Cynomolgus Macaque with Epistaxis.";
RL Genome Announc. 1:E00188-12(2013).
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}.
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:ELA08251.1}.
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DR EMBL; ANIN01000002; ELA08251.1; -; Genomic_DNA.
DR AlphaFoldDB; L2F644; -.
DR STRING; 1230338.MOMA_06806; -.
DR PATRIC; fig|1230338.3.peg.1453; -.
DR eggNOG; COG1364; Bacteria.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000023795; 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:UP000023795};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01106}.
FT CHAIN 1..193
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT /id="PRO_5023266181"
FT CHAIN 194..400
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT /id="PRO_5023266180"
FT ACT_SITE 194
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT SITE 116
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 117
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 193..194
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
SQ SEQUENCE 400 AA; 42972 MW; FAD9813B4F2908B1 CRC64;
MPVGNVNLSK LLPIKGIKIG VTEAHIRYPN RKDLTVFEIC QHASVAVVTT QNQFCASPVK
LVREFIKTDT PRYLLINTGN ANAGTGKDGD MRALATCQAL ANKTGVKPSQ VLPYSTGVIG
ETLPSDKIIA GLDKLLANLT HSQAQDNWLN CAYSIMTTDT IPKGHSETVT IDDITYTVTG
VSKGAGMIRP NMATMLGFVA TDANIDKNLL QDMLIKIVNK TFNRISVDGD TSTNDCCTLI
ATGQVGDLID SENHAHYMPI YQAIYKVMLT IATLIVRDGE GATKFITVKV TGGKNTADCT
KIAYSIAHSP LVKTAFFASD PNWGRILAAA GYAGVDFDQS KVSVALDEVK ICERGGLADG
YTEPLGLEVM TRPEITIHID LGCGGGQVIQ CILVIYHTIM
//
