ARGA_MYCTU
ID ARGA_MYCTU Reviewed; 174 AA.
AC O33289; F2GPH5; L0TAR8;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Amino-acid acetyltransferase;
DE EC=2.3.1.1;
DE AltName: Full=N-acetylglutamate synthase;
DE Short=AGS;
DE Short=NAGS;
GN Name=argA; OrderedLocusNames=Rv2747;
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBSTRATE SPECIFICITY, MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=15838030; DOI=10.1128/jb.187.9.3039-3044.2005;
RA Errey J.C., Blanchard J.S.;
RT "Functional characterization of a novel ArgA from Mycobacterium
RT tuberculosis.";
RL J. Bacteriol. 187:3039-3044(2005).
RN [3]
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 [4]
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).
CC -!- FUNCTION: Catalyzes the conversion of L-glutamate to alpha-N-acetyl-L-
CC glutamate. L-glutamine is a significantly better substrate compared to
CC L-glutamate. {ECO:0000269|PubMed:15838030}.
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:0000269|PubMed:15838030};
CC -!- ACTIVITY REGULATION: Inhibited by L-arginine.
CC {ECO:0000269|PubMed:15838030}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=150 mM for acetyl-CoA {ECO:0000269|PubMed:15838030};
CC KM=280 mM for glutamine {ECO:0000269|PubMed:15838030};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4.
CC -!- SUBUNIT: Homodimer and homotetramer. {ECO:0000269|PubMed:15838030}.
CC -!- MASS SPECTROMETRY: Mass=20978; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15838030};
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45546.1; -; Genomic_DNA.
DR PIR; B70879; B70879.
DR RefSeq; NP_217263.1; NC_000962.3.
DR RefSeq; WP_003414037.1; NZ_NVQJ01000020.1.
DR PDB; 5YGE; X-ray; 2.04 A; A/B=2-174.
DR PDB; 5YO2; X-ray; 3.00 A; A/B=1-174.
DR PDB; 6ADD; X-ray; 2.30 A; A/B=1-174.
DR PDBsum; 5YGE; -.
DR PDBsum; 5YO2; -.
DR PDBsum; 6ADD; -.
DR AlphaFoldDB; O33289; -.
DR SMR; O33289; -.
DR STRING; 83332.Rv2747; -.
DR PaxDb; O33289; -.
DR DNASU; 888407; -.
DR GeneID; 45426734; -.
DR GeneID; 888407; -.
DR KEGG; mtu:Rv2747; -.
DR TubercuList; Rv2747; -.
DR eggNOG; COG1246; Bacteria.
DR InParanoid; O33289; -.
DR OMA; IQEFWVA; -.
DR PhylomeDB; O33289; -.
DR BRENDA; 2.3.1.1; 3445.
DR SABIO-RK; O33289; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IDA:MTBBASE.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:MTBBASE.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IDA:MTBBASE.
DR GO; GO:0051289; P:protein homotetramerization; IPI:MTBBASE.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Amino-acid biosynthesis;
KW Arginine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..174
FT /note="Amino-acid acetyltransferase"
FT /id="PRO_0000420585"
FT DOMAIN 10..148
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:5YGE"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:5YGE"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:5YGE"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:5YGE"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:5YGE"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:5YGE"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:5YGE"
FT TURN 56..60
FT /evidence="ECO:0007829|PDB:5YGE"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:5YGE"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:5YGE"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:5YGE"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6ADD"
FT HELIX 92..106
FT /evidence="ECO:0007829|PDB:5YGE"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:5YGE"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:5YGE"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:5YGE"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6ADD"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:5YGE"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:5YGE"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:5YGE"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:6ADD"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:5YGE"
SQ SEQUENCE 174 AA; 19589 MW; 48E20A38757B7EBE CRC64;
MTERPRDCRP VVRRARTSDV PAIKQLVDTY AGKILLEKNL VTLYEAVQEF WVAEHPDLYG
KVVGCGALHV LWSDLGEIRT VAVDPAMTGH GIGHAIVDRL LQVARDLQLQ RVFVLTFETE
FFARHGFTEI EGTPVTAEVF DEMCRSYDIG VAEFLDLSYV KPNILGNSRM LLVL
