ID A0A1B1BHQ0_9MICO Unreviewed; 394 AA.
AC A0A1B1BHQ0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 05-JUN-2019, entry version 19.
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=PA27867_1179 {ECO:0000313|EMBL:ANP72145.1};
OS Cryobacterium arcticum.
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=670052 {ECO:0000313|EMBL:ANP72145.1, ECO:0000313|Proteomes:UP000092582};
RN [1] {ECO:0000313|EMBL:ANP72145.1, ECO:0000313|Proteomes:UP000092582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27867 {ECO:0000313|EMBL:ANP72145.1,
RC ECO:0000313|Proteomes:UP000092582};
RA Lee J., Kim O.-S.;
RT "Genome sequencing of Cryobacterium arcticum PAMC 27867.";
RL Submitted (JUN-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; CP016282; ANP72145.1; -; Genomic_DNA.
DR RefSeq; WP_066594410.1; NZ_CP016282.1.
DR EnsemblBacteria; ANP72145; ANP72145; PA27867_1179.
DR KEGG; cart:PA27867_1179; -.
DR PATRIC; fig|670052.7.peg.1221; -.
DR KO; K00620; -.
DR OrthoDB; 1083409at2; -.
DR BioCyc; GCF_001679725:G1EX2-1205-MONOMER; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000092582; Chromosome 1.
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:UP000092582};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW Reference proteome {ECO:0000313|Proteomes:UP000092582};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01106}.
FT ACT_SITE 187 187 Nucleophile. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 153 153 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 176 176 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 187 187 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 267 267 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 389 389 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 394 394 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT SITE 109 109 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 110 110 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 186 187 Cleavage; by autolysis.
FT {ECO:0000256|HAMAP-Rule:MF_01106}.
SQ SEQUENCE 394 AA; 39995 MW; 2D7BED66C4974A6B CRC64;
MSVTAPAGFA AAGVTAGLKK SGGLDLAIVS NLGPLANAAT VFTSNRCKAN PIIWSQQVMR
DGRVSAIVLN SGGANCYTGT IGFQTTHATA EAVADQLQVS AGDVLVCSTG LIGEQLDLGK
LTAGVLDAGL ALRDTAASSS ADAGLAAAQA IMTTDTRPKQ ATRVSPAGWT IGGMAKGAGM
LAPGLATMLV VITTDAVLTS AQLDAALREA TRVTFDRLDS DGCMSTNDTV SLLASGASGV
DADPAEFAAA LTELCRDLTL QLQGDAEGAS HDVAITVRNS ASETEAVTVA RAVSRSNLFK
AAIYGNDPNW GRVLAAVGTI PEADAAFDPY GIDVAINGIQ VCTAGEPDQP RELVDLAPRA
VSVVIDLHAG TAGATIWTND LTHDYVEENS AYSS
//
