ID A0A143PIF4_9BACT Unreviewed; 402 AA.
AC A0A143PIF4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 05-JUN-2019, entry version 25.
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:AMY07554.1};
GN ORFNames=LuPra_00727 {ECO:0000313|EMBL:AMY07554.1};
OS Luteitalea pratensis.
OC Bacteria; Acidobacteria; Vicinamibacteria; Vicinamibacteraceae;
OC Luteitalea.
OX NCBI_TaxID=1855912 {ECO:0000313|EMBL:AMY07554.1, ECO:0000313|Proteomes:UP000076079};
RN [1] {ECO:0000313|EMBL:AMY07554.1, ECO:0000313|Proteomes:UP000076079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100886 HEG_-6_39 {ECO:0000313|Proteomes:UP000076079};
RX PubMed=27231379;
RA Huang S., Vieira S., Bunk B., Riedel T., Sproer C., Overmann J.;
RT "First Complete Genome Sequence of a Subdivision 6 Acidobacterium
RT Strain.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100886 HEG_-6_39 {ECO:0000313|Proteomes:UP000076079};
RA Huang S., Vieira S., Bunk B., Riedel T., Sproeer C., Overmann J.;
RT "First Complete Genome Sequence of a Subdivision 6 Acidobacterium.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes two activities which are involved in the
CC cyclic version of arginine biosynthesis: the synthesis of N-
CC acetylglutamate from glutamate and acetyl-CoA as the acetyl donor,
CC and of ornithine by transacetylation between N(2)-acetylornithine
CC and glutamate. {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;
CC EC=2.3.1.35; Evidence={ECO:0000256|HAMAP-Rule:MF_01106};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-
CC glutamate; Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.1.1; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01106};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-
CC acetyl-L-ornithine (cyclic): step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_01106}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC acetyl-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|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
CC biosynthetic pathway. {ECO:0000256|HAMAP-Rule:MF_01106}.
CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000256|HAMAP-
CC Rule:MF_01106}.
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DR EMBL; CP015136; AMY07554.1; -; Genomic_DNA.
DR EnsemblBacteria; AMY07554; AMY07554; LuPra_00727.
DR KEGG; abac:LuPra_00727; -.
DR PATRIC; fig|1813736.3.peg.762; -.
DR KO; K00620; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000076079; 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; -; 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 {ECO:0000256|HAMAP-Rule:MF_01106};
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106};
KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01106};
KW Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_01106};
KW Complete proteome {ECO:0000313|Proteomes:UP000076079};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW Reference proteome {ECO:0000313|Proteomes:UP000076079};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01106}.
FT ACT_SITE 191 191 Nucleophile. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 154 154 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 180 180 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 191 191 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 274 274 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 397 397 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 402 402 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT SITE 117 117 Involved in the stabilization of negative
FT charge on the oxyanion by the formation
FT of the oxyanion hole. {ECO:0000256|HAMAP-
FT Rule:MF_01106}.
FT SITE 118 118 Involved in the stabilization of negative
FT charge on the oxyanion by the formation
FT of the oxyanion hole. {ECO:0000256|HAMAP-
FT Rule:MF_01106}.
FT SITE 190 191 Cleavage; by autolysis.
FT {ECO:0000256|HAMAP-Rule:MF_01106}.
SQ SEQUENCE 402 AA; 42015 MW; 3B18EDCC8457476F CRC64;
MITHIEGGIT APAGFRAAGV HCGIKANPEK LDLALLVSDL PATAAAVFTT NLAVAPPVIV
SRDHLHATRG HARAVVVNSG CANACTGDQG RQVAHLMAAE TARAIDCDLE EVIVMSTGVI
GVQLDPRTVT HGIIAATDVL SVDGHMRCAQ AIMTTDPFPK ERAVEVTTTR GTFRIGGICK
GSGMIEPRMA TMLGVLTCDA AVSPVLLQRV LSEVTEHTFN AITVDGECST NDCVALLANG
ASGVTIGEAD LPLFSDALYE VCKFLSTEIV RGGEGATKLV TVQVTGARSY DEAKQAARAI
ANSLLVKTAI HGGDPNWGRL VAVAGRAGVG FDLQAAAVRI GDVVLFEGGR PFDERAPQAA
AYLQRKDITV GVDLGTGGTH EATMWTCDLS EEYVQINAEY RT
//
