ARGJ_MYCTU
ID ARGJ_MYCTU Reviewed; 404 AA.
AC P9WPZ3; L0TA91; P63571; P94988;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
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=Rv1653; ORFNames=MTCY06H11.18;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-404 IN COMPLEX WITH SUBSTRATE
RP ANALOGS, AND SUBUNIT.
RX PubMed=20184895; DOI=10.1016/j.jmb.2010.02.018;
RA Sankaranarayanan R., Cherney M.M., Garen C., Garen G., Niu C., Yuan M.,
RA James M.N.;
RT "The molecular structure of ornithine acetyltransferase from Mycobacterium
RT tuberculosis bound to ornithine, a competitive inhibitor.";
RL J. Mol. Biol. 397:979-990(2010).
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 -!- 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|PubMed:20184895}.
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 -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP44418.1; -; Genomic_DNA.
DR PIR; H70620; H70620.
DR RefSeq; NP_216169.1; NC_000962.3.
DR RefSeq; WP_003408160.1; NZ_NVQJ01000069.1.
DR PDB; 3IT4; X-ray; 1.70 A; A/C=2-199, B/D=200-404.
DR PDB; 3IT6; X-ray; 2.40 A; A/C=2-199, B/D=200-404.
DR PDBsum; 3IT4; -.
DR PDBsum; 3IT6; -.
DR AlphaFoldDB; P9WPZ3; -.
DR SMR; P9WPZ3; -.
DR STRING; 83332.Rv1653; -.
DR PaxDb; P9WPZ3; -.
DR DNASU; 885125; -.
DR GeneID; 885125; -.
DR KEGG; mtu:Rv1653; -.
DR TubercuList; Rv1653; -.
DR eggNOG; COG1364; Bacteria.
DR OMA; DYVHENS; -.
DR PhylomeDB; P9WPZ3; -.
DR BRENDA; 2.3.1.35; 3445.
DR UniPathway; UPA00068; UER00106.
DR UniPathway; UPA00068; UER00111.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IBA:GO_Central.
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 GO; GO:0006592; P:ornithine biosynthetic process; IBA:GO_Central.
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..199
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002193"
FT CHAIN 200..404
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002194"
FT ACT_SITE 200
FT /note="Nucleophile"
FT BINDING 166
FT /ligand="substrate"
FT BINDING 189
FT /ligand="substrate"
FT BINDING 200
FT /ligand="substrate"
FT BINDING 280
FT /ligand="substrate"
FT BINDING 399
FT /ligand="substrate"
FT BINDING 404
FT /ligand="substrate"
FT SITE 127
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT SITE 128
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT SITE 199..200
FT /note="Cleavage; by autolysis"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3IT6"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3IT4"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:3IT4"
FT HELIX 92..113
FT /evidence="ECO:0007829|PDB:3IT4"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:3IT4"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3IT4"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:3IT4"
FT HELIX 213..226
FT /evidence="ECO:0007829|PDB:3IT4"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:3IT4"
FT HELIX 257..277
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 285..295
FT /evidence="ECO:0007829|PDB:3IT4"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:3IT4"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:3IT4"
FT HELIX 323..330
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:3IT4"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:3IT4"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 368..376
FT /evidence="ECO:0007829|PDB:3IT4"
FT STRAND 382..389
FT /evidence="ECO:0007829|PDB:3IT4"
FT HELIX 393..400
FT /evidence="ECO:0007829|PDB:3IT4"
SQ SEQUENCE 404 AA; 41147 MW; 7BD0CCD5FB8DE634 CRC64;
MTDLAGTTRL LRAQGVTAPA GFRAAGVAAG IKASGALDLA LVFNEGPDYA AAGVFTRNQV
KAAPVLWTQQ VLTTGRLRAV ILNSGGANAC TGPAGFADTH ATAEAVAAAL SDWGTETGAI
EVAVCSTGLI GDRLPMDKLL AGVAHVVHEM HGGLVGGDEA AHAIMTTDNV PKQVALHHHD
NWTVGGMAKG AGMLAPSLAT MLCVLTTDAA AEPAALERAL RRAAAATFDR LDIDGSCSTN
DTVLLLSSGA SEIPPAQADL DEAVLRVCDD LCAQLQADAE GVTKRVTVTV TGAATEDDAL
VAARQIARDS LVKTALFGSD PNWGRVLAAV GMAPITLDPD RISVSFNGAA VCVHGVGAPG
AREVDLSDAD IDITVDLGVG DGQARIRTTD LSHAYVEENS AYSS
