ARGJ_ALKHC
ID ARGJ_ALKHC Reviewed; 411 AA.
AC Q9K8V3;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ;
DE Includes:
DE RecName: Full=Glutamate N-acetyltransferase;
DE EC=2.3.1.35;
DE AltName: Full=Ornithine acetyltransferase;
DE Short=OATase;
DE AltName: Full=Ornithine transacetylase;
DE Includes:
DE RecName: Full=Amino-acid acetyltransferase;
DE EC=2.3.1.1;
DE AltName: Full=N-acetylglutamate synthase;
DE Short=AGSase;
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain;
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain;
GN Name=argJ; OrderedLocusNames=BH2899;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of arginine biosynthesis bifunctional protein argj
RT (10175521) from bacillus halodurans at 2.00 a resolution.";
RL Submitted (JUL-2011) to the PDB data bank.
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:0000250}.
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 -!- 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 -!- ACTIVITY REGULATION: Feedback inhibition by L-ornithine. {ECO:0000250}.
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.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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:0000305}.
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DR EMBL; BA000004; BAB06618.1; -; Genomic_DNA.
DR PIR; C84012; C84012.
DR PDB; 1VRA; X-ray; 2.00 A; A=1-196, B=197-411.
DR PDBsum; 1VRA; -.
DR AlphaFoldDB; Q9K8V3; -.
DR SMR; Q9K8V3; -.
DR STRING; 272558.10175521; -.
DR MEROPS; T05.002; -.
DR EnsemblBacteria; BAB06618; BAB06618; BAB06618.
DR KEGG; bha:BH2899; -.
DR eggNOG; COG1364; Bacteria.
DR HOGENOM; CLU_027172_1_0_9; -.
DR OMA; DYVHENS; -.
DR OrthoDB; 1083409at2; -.
DR UniPathway; UPA00068; UER00106.
DR UniPathway; UPA00068; UER00111.
DR EvolutionaryTrace; Q9K8V3; -.
DR Proteomes; UP000001258; 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 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Amino-acid biosynthesis;
KW Arginine biosynthesis; Autocatalytic cleavage; Cytoplasm;
KW Multifunctional enzyme; Reference proteome; Transferase.
FT CHAIN 1..196
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002113"
FT CHAIN 197..411
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002114"
FT ACT_SITE 197
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 123
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000250"
FT SITE 124
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000250"
FT SITE 196..197
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 40..56
FT /evidence="ECO:0007829|PDB:1VRA"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 76..87
FT /evidence="ECO:0007829|PDB:1VRA"
FT HELIX 93..111
FT /evidence="ECO:0007829|PDB:1VRA"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:1VRA"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1VRA"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 177..186
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:1VRA"
FT HELIX 210..223
FT /evidence="ECO:0007829|PDB:1VRA"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:1VRA"
FT HELIX 260..280
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 288..298
FT /evidence="ECO:0007829|PDB:1VRA"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:1VRA"
FT HELIX 313..320
FT /evidence="ECO:0007829|PDB:1VRA"
FT HELIX 326..335
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:1VRA"
FT HELIX 365..374
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 376..383
FT /evidence="ECO:0007829|PDB:1VRA"
FT STRAND 386..396
FT /evidence="ECO:0007829|PDB:1VRA"
FT HELIX 400..406
FT /evidence="ECO:0007829|PDB:1VRA"
SQ SEQUENCE 411 AA; 43479 MW; 0D2D057189397A27 CRC64;
MNVINETANV LKLETGSVTS AKGFSAVGIH TGVKRKRKDL GAIVCEVPAS SAAVYTLNKV
QAAPLKVTQE SIAVEGKLQA MIVNSGIANA CTGKRGLDDA YTMRAVGAET FHIPEHYVAV
TSTGVIGEFL PMDVITNGIR QLKPEATIEG AHAFNEAILT TDTVEKHTCY QTIVNGKTVT
VGGVAKGSGM IHPNMATMLS FVTTDANIDH GHLQGALSAI TNETFNRITV DGDTSTNDMV
VVMASGLAEN EALTPEHPDW ANFYKALQLA CEDLAKQIAR DGEGATKLIE VEVTGAANDQ
EAGMVAKQIV GSDLVKTAIY GADANWGRII CAIGYSGCEV NQETIDIAIG PIVTLKQSEP
TGFSEEEATA YLKEADPVKI SVNLHIGNGT GKAWGCDLTY DYVRINAGYR T
