ARGJ_BACAN
ID ARGJ_BACAN Reviewed; 407 AA.
AC Q81M96; Q6HTP9; Q6KMY8;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ {ECO:0000255|HAMAP-Rule:MF_01106};
DE Includes:
DE RecName: Full=Glutamate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE EC=2.3.1.35 {ECO:0000255|HAMAP-Rule:MF_01106};
DE AltName: Full=Ornithine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE Short=OATase {ECO:0000255|HAMAP-Rule:MF_01106};
DE AltName: Full=Ornithine transacetylase {ECO:0000255|HAMAP-Rule:MF_01106};
DE Includes:
DE RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01106};
DE EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_01106};
DE AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_01106};
DE Short=AGSase {ECO:0000255|HAMAP-Rule:MF_01106};
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000255|HAMAP-Rule:MF_01106};
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000255|HAMAP-Rule:MF_01106};
GN Name=argJ {ECO:0000255|HAMAP-Rule:MF_01106};
GN OrderedLocusNames=BA_4354, GBAA_4354, BAS4039;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) 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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-
CC Rule:MF_01106}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC {ECO:0000255|HAMAP-Rule:MF_01106}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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.
CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC Rule:MF_01106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT56340.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE016879; AAP28072.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33474.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT56340.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_846586.1; NC_003997.3.
DR RefSeq; WP_000598413.1; NZ_WXXJ01000027.1.
DR RefSeq; YP_030289.1; NC_005945.1.
DR AlphaFoldDB; Q81M96; -.
DR SMR; Q81M96; -.
DR IntAct; Q81M96; 1.
DR STRING; 260799.BAS4039; -.
DR MEROPS; T05.002; -.
DR DNASU; 1087579; -.
DR EnsemblBacteria; AAP28072; AAP28072; BA_4354.
DR EnsemblBacteria; AAT33474; AAT33474; GBAA_4354.
DR GeneID; 45024019; -.
DR KEGG; ban:BA_4354; -.
DR KEGG; bar:GBAA_4354; -.
DR KEGG; bat:BAS4039; -.
DR PATRIC; fig|198094.11.peg.4322; -.
DR eggNOG; COG1364; Bacteria.
DR HOGENOM; CLU_027172_1_0_9; -.
DR OMA; DYVHENS; -.
DR UniPathway; UPA00068; UER00106.
DR UniPathway; UPA00068; UER00111.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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; Amino-acid biosynthesis; Arginine biosynthesis;
KW Autocatalytic cleavage; Cytoplasm; Multifunctional enzyme;
KW Reference proteome; Transferase.
FT CHAIN 1..193
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT /id="PRO_0000002103"
FT CHAIN 194..407
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT /id="PRO_0000002104"
FT ACT_SITE 194
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 402
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01106"
FT SITE 193..194
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01106"
SQ SEQUENCE 407 AA; 43740 MW; BC3C984B1A18530B CRC64;
MIKVASITKV EDGSIVTPKG FSAIGTAIGL KKGKKDLGAI VCDVPASCAA VYTTNQIQAA
PLQVTKDSIT TEGKLQAIIV NSGNANACTG MKGLQDAYEM RALGAEHFGL KEKYVAVAST
GVIGVPLPMD IIRKGIVTLI PAKEENGAHS FSEAILTTDL ITKETCYEMI IDGKKVMIAG
VAKGSGMIHP NMATMLSFIT TDARIEHDVL QTALSQITNH TFNQITVDGD TSTNDMVIAM
ASGLSETKPI DMEHADWETF VFALQKVCED LAKKIAQDGE GATKLIEVNV LGVQTNEEAK
KIAKQIVGSS LVKTAIHGED PNWGRIISSI GQSEVAINPN TIDITLQSIS VLKNSEPQTF
SEEEMKERLQ EDEIVINVYL HLGKETGSAW GCDLSYEYVK INACYRT
