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Database: UniProt
Entry: B0PD04_9FIRM
LinkDB: B0PD04_9FIRM
Original site: B0PD04_9FIRM 
ID   B0PD04_9FIRM            Unreviewed;       406 AA.
AC   B0PD04;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   26-FEB-2020, entry version 71.
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:EDS10690.1};
GN   ORFNames=ANACOL_02667 {ECO:0000313|EMBL:EDS10690.1};
OS   Anaerotruncus colihominis DSM 17241.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Anaerotruncus.
OX   NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS10690.1, ECO:0000313|Proteomes:UP000003803};
RN   [1] {ECO:0000313|EMBL:EDS10690.1, ECO:0000313|Proteomes:UP000003803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS10690.1,
RC   ECO:0000313|Proteomes:UP000003803};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Anaerotruncus colihominis(DSM 17241).";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS10690.1, ECO:0000313|Proteomes:UP000003803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS10690.1,
RC   ECO:0000313|Proteomes:UP000003803};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2007) 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:EDS10690.1}.
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DR   EMBL; ABGD02000022; EDS10690.1; -; Genomic_DNA.
DR   RefSeq; WP_006873327.1; NZ_DS544172.1.
DR   STRING; 445972.ANACOL_02667; -.
DR   MEROPS; T05.002; -.
DR   EnsemblBacteria; EDS10690; EDS10690; ANACOL_02667.
DR   eggNOG; ENOG4105C5V; Bacteria.
DR   eggNOG; COG1364; LUCA.
DR   HOGENOM; CLU_027172_1_0_9; -.
DR   OrthoDB; 1083409at2; -.
DR   BioCyc; GCF_000154565-HMP:ANACOL_RS01540-MONOMER; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000003803; 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   ECO:0000313|EMBL:EDS10690.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000003803};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01106, ECO:0000313|EMBL:EDS10690.1}.
FT   CHAIN           1..188
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ
FT                   alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT                   /id="PRO_5023445587"
FT   CHAIN           189..406
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT                   chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT                   /id="PRO_5023445586"
FT   ACT_SITE        189
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         152
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         178
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         189
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         275
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         401
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         406
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   SITE            115
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            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            188..189
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
SQ   SEQUENCE   406 AA;  42117 MW;  3D789B7E25BF3615 CRC64;
     MAFTFVEGGV CAAQGFSAGA VHAGIRKNHD KKDLALIFAD RMCSAAAIYT QNKVKGAPLI
     VTREHLQNGR ARAILCNSGN ANTCNADGLD IAAAMCKSAA QALKIAANDV VVASTGVIGQ
     PLPLGPIKDA MPALAASLST GGSGDAAEAI MTTDTKRKQV AVRFPIGDKL CTIGGIAKGS
     GMIHPNMATM LCFVTTDADI APELLQKACK DVADETFNMI SVDGDTSTND MLAILASGAA
     ANEPIKSLGK EYYHFQQGLM IVCRRLAREL AADGEGATKL LECAVTGAPD CQTAKKVAKS
     VICSSLFKAA MFGGDANWGR VLCAIGYTDA EFDVSRVGVT LSSAAGSVPV CSNGAGVPFS
     EEQAAKILAQ PEIRIEIDMA QGGETATAWG CDLTYDYVKI NGDYRT
//
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