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Database: UniProt
Entry: A0A1Z8WSM0_9CHLR
LinkDB: A0A1Z8WSM0_9CHLR
Original site: A0A1Z8WSM0_9CHLR 
ID   A0A1Z8WSM0_9CHLR        Unreviewed;       404 AA.
AC   A0A1Z8WSM0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   11-DEC-2019, entry version 11.
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=CBC30_05570 {ECO:0000313|EMBL:OUU74496.1};
OS   Chloroflexi bacterium TMED70.
OC   Bacteria; Chloroflexi.
OX   NCBI_TaxID=1986676 {ECO:0000313|EMBL:OUU74496.1, ECO:0000313|Proteomes:UP000196464};
RN   [1] {ECO:0000313|EMBL:OUU74496.1, ECO:0000313|Proteomes:UP000196464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED70 {ECO:0000313|EMBL:OUU74496.1};
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   Submitted (MAY-2017) 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|HAMAP-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|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|HAMAP-
CC       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:OUU74496.1}.
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DR   EMBL; NHDX01000036; OUU74496.1; -; Genomic_DNA.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000196464; 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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01106};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01106, ECO:0000313|EMBL:OUU74496.1}.
FT   CHAIN           1..191
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ
FT                   alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT                   /id="PRO_5023534162"
FT   CHAIN           192..404
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT                   chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT                   /id="PRO_5023534163"
FT   ACT_SITE        192
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         155
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         181
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         192
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         277
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         399
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         404
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   SITE            120
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            121
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            191..192
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
SQ   SEQUENCE   404 AA;  43299 MW;  2FE86CAF6C55E22F CRC64;
     MESEIKINKK GDICSPKGFL SGSIFSGIKS PGQDKRDIGI IYSESDCISA GTFTQNSVVS
     PSVTWTKDIT SNGNVKAIVA NSGCANCAVG EQGLIDAKEM ASIAANSLGI DQKEVAVAST
     GIIGVELPMA LMRKFIPEIK MSKKDGNGFA RSILTTDTKT KEISVSFEID GTEINVAGVA
     KGSGMIHPNM ATMLAFITSD XDIEKPXLQK ILKNSVNKSF NQISVDGDQS TNDTVLLLAN
     GMAKNKKINT ENDSKKFIEA LDIVCTFLAQ EIAKDGEGNT RLIEATVTGA KTEEDAMLAS
     RFIVTSNLVK TAVYGRDPNW GRIIMALGAS QIPLDESKIE IFVNDIQIVS EGIAISYNHQ
     SIVIAMGEEL IRFKINLNIG SESGVAWGSE LTEEYVVFNS AYTT
//
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