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Database: UniProt
Entry: A7I4D3_METB6
LinkDB: A7I4D3_METB6
Original site: A7I4D3_METB6 
ID   A7I4D3_METB6            Unreviewed;       385 AA.
AC   A7I4D3;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   26-FEB-2020, entry version 87.
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   OrderedLocusNames=Mboo_0070 {ECO:0000313|EMBL:ABS54594.1};
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442 {ECO:0000313|EMBL:ABS54594.1, ECO:0000313|Proteomes:UP000002408};
RN   [1] {ECO:0000313|EMBL:ABS54594.1, ECO:0000313|Proteomes:UP000002408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8
RC   {ECO:0000313|Proteomes:UP000002408};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zinder S., Richardson P.;
RT   "Complete sequence of Candidatus Methanoregula boonei 6A8.";
RL   Submitted (JUL-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}.
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DR   EMBL; CP000780; ABS54594.1; -; Genomic_DNA.
DR   RefSeq; WP_011991082.1; NC_009712.1.
DR   STRING; 456442.Mboo_0070; -.
DR   MEROPS; T05.002; -.
DR   EnsemblBacteria; ABS54594; ABS54594; Mboo_0070.
DR   GeneID; 5411719; -.
DR   KEGG; mbn:Mboo_0070; -.
DR   eggNOG; arCOG04413; Archaea.
DR   eggNOG; COG1364; LUCA.
DR   HOGENOM; CLU_027172_1_0_2; -.
DR   KO; K00620; -.
DR   OMA; GMIAPNM; -.
DR   OrthoDB; 29910at2157; -.
DR   BioCyc; MBOO456442:G1G9N-71-MONOMER; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000002408; 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   ECO:0000313|EMBL:ABS54594.1};
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:UP000002408};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01106, ECO:0000313|EMBL:ABS54594.1}.
FT   CHAIN           1..175
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ
FT                   alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT                   /id="PRO_5023216013"
FT   CHAIN           176..385
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT                   chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT                   /id="PRO_5023216014"
FT   ACT_SITE        176
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         143
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         165
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         176
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         255
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         380
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   BINDING         385
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
FT   SITE            104
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            105
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            175..176
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01106"
SQ   SEQUENCE   385 AA;  40451 MW;  D465F24F0F478F8A CRC64;
     MAYKSLCAVK GVTANGIKEG KFGLALIRAS GTSAGVFTAN LARAAPIELM RKQIRKGRLE
     AVIANSGCAN AYTGRRGYDD AVSMTEYAGS ALGVDTSSVG VASTGVIGRY LDLPLIRRQC
     ADVALNLTSS PAAEDLTVKA IMTTDLYPKH ALVEKEDFTI GAIAKGSGMI APNMGTMLAF
     IYTDAEIAAQ PLREALRAAT RRTFNRVVVD GDTSTNDIAL CTATGESGKV NTTEFSAALE
     ACCRSLAQQI AADGEGASKL LEVTVRGAPK EEAAAKVARV VIESPLVKTA VYGEDPNWGR
     VIAAAGRAGV KFDPNAVSLW ISDGNEKYPL VKSGEIIADL TKAKAAMHGK KVIFILDLGA
     GKEEATAWGC DLTEKYVEIN GRYTT
//
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