ID A0A1N6HHN8_9RHOB Unreviewed; 407 AA.
AC A0A1N6HHN8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 05-JUN-2019, entry version 15.
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=SAMN05444002_3392 {ECO:0000313|EMBL:SIO19368.1};
OS Oceanicola litoreus.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Oceanicola.
OX NCBI_TaxID=1217970 {ECO:0000313|EMBL:SIO19368.1, ECO:0000313|Proteomes:UP000184932};
RN [1] {ECO:0000313|EMBL:SIO19368.1, ECO:0000313|Proteomes:UP000184932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29440 {ECO:0000313|EMBL:SIO19368.1,
RC ECO:0000313|Proteomes:UP000184932};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FSRL01000001; SIO19368.1; -; Genomic_DNA.
DR RefSeq; WP_074257298.1; NZ_FSRL01000001.1.
DR BioCyc; GCF_900142295:BUR94_RS16710-MONOMER; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000184932; 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; -; 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:UP000184932};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW Reference proteome {ECO:0000313|Proteomes:UP000184932};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01106,
KW ECO:0000313|EMBL:SIO19368.1}.
FT ACT_SITE 198 198 Nucleophile. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 161 161 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 187 187 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 198 198 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 279 279 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 402 402 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT BINDING 407 407 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01106}.
FT SITE 124 124 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 125 125 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 197 198 Cleavage; by autolysis.
FT {ECO:0000256|HAMAP-Rule:MF_01106}.
SQ SEQUENCE 407 AA; 42429 MW; C85128D86FC7B5AE CRC64;
MGKYPVSPLA PEKFPDLPVI KGVRFAAVEA GVRYADRLDV MLAVLDPGSV VAGVFTRSST
RSAPVRDCEA KLRKVSEAGA AILVNSGNSN AFTGSAGQES VEAICAAVAE AADVPKGRVF
TSSTGVIGER LPHDRITAKV GELVEALDEG GIARAAQAIM TTDTFAKGAT REIELKGGVV
KIAGIAKGSG MIAPDMATML VYIFTDAKVS RDALQAMVSC HNETTFNAIT VDGDTSTSDT
LICAATGASG VDCDDSEEFE AALKAVMKDL AHQVVKDGEG ATKFVAVKVT GAAHDADAKR
VAMSIANSPL VKTAIAGEDP NWGRIVAAVG KSGAEADRDK LTIRFGEVLV AERGWVAPGY
SEEQAAGYMK LPELVIGVDL GLGKGRFTAW TCDLTHQYIS INADYRS
//
