ARGJ_POPTR
ID ARGJ_POPTR Reviewed; 481 AA.
AC B9NAN0; U5FU53;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03124};
DE Includes:
DE RecName: Full=Glutamate N-acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03124};
DE Short=GAT {ECO:0000255|HAMAP-Rule:MF_03124};
DE EC=2.3.1.35 {ECO:0000255|HAMAP-Rule:MF_03124};
DE AltName: Full=Ornithine acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03124};
DE Short=OATase {ECO:0000255|HAMAP-Rule:MF_03124};
DE AltName: Full=Ornithine transacetylase {ECO:0000255|HAMAP-Rule:MF_03124};
DE Includes:
DE RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_03124};
DE EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_03124};
DE AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_03124};
DE Short=AGS {ECO:0000255|HAMAP-Rule:MF_03124};
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000255|HAMAP-Rule:MF_03124};
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000255|HAMAP-Rule:MF_03124};
DE Flags: Precursor;
GN ORFNames=POPTRDRAFT_746969;
OS Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp.
OS trichocarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=3694;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nisqually;
RX PubMed=16973872; DOI=10.1126/science.1128691;
RA Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W.,
RA Brun A., Brunner A., Busov V., Campbell M., Carlson J., Chalot M.,
RA Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S.,
RA Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A.,
RA dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S.,
RA Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J.,
RA Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y.,
RA Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S.,
RA Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J.,
RA Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F.,
RA Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O.,
RA Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J.,
RA Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J.,
RA Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A.,
RA Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S.,
RA Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y.,
RA Rokhsar D.S.;
RT "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL Science 313:1596-1604(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nisqually;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Grigoriev I.V., Terry A., Salamov A.A., Otillar R., Lou Y., Lucas S.,
RA Hammon N., Glavina del Rio T., Detter J., Kalin E., Tice H., Pitluck S.,
RA Chapman J., Putnam N.H., Brunner A., Busov V., Campbell M., Chalot M.,
RA Covert S., Davis J., DiFazio S., Gribskov M., Gunter L., Hamberger B.,
RA Jansson S., Joshi C., Larimer F., Martin F., Napoli C., Nelson D.,
RA Ralph S., Rombauts S., Rouze P., Schrader J., Tsai C., Vahala J.,
RA Tuskan G., Rokhsar D.;
RL Submitted (DEC-2008) 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 acetylglutamate from
CC glutamate and acetyl-CoA, and of ornithine by transacetylation between
CC acetylornithine and glutamate. {ECO:0000255|HAMAP-Rule:MF_03124}.
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_03124};
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_03124};
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_03124}.
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_03124}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000255|HAMAP-
CC Rule:MF_03124}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_03124}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03124}.
CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC Rule:MF_03124}.
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DR EMBL; CM009301; ERP54763.1; -; Genomic_DNA.
DR RefSeq; XP_006376966.1; XM_006376904.1.
DR AlphaFoldDB; B9NAN0; -.
DR SMR; B9NAN0; -.
DR STRING; 3694.POPTR_0012s11640.1; -.
DR PRIDE; B9NAN0; -.
DR GeneID; 18103861; -.
DR KEGG; pop:18103861; -.
DR eggNOG; KOG2786; Eukaryota.
DR HOGENOM; CLU_027172_1_1_1; -.
DR InParanoid; B9NAN0; -.
DR UniPathway; UPA00068; UER00106.
DR UniPathway; UPA00068; UER00111.
DR Proteomes; UP000006729; Chromosome 12.
DR ExpressionAtlas; B9NAN0; baseline.
DR GO; GO:0009507; C:chloroplast; 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 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW Autocatalytic cleavage; Chloroplast; Multifunctional enzyme; Plastid;
KW Reference proteome; Transferase.
FT CHAIN 1..261
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT /id="PRO_0000397986"
FT CHAIN 262..481
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT /id="PRO_0000397987"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 476
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT BINDING 481
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT SITE 186
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_03124"
FT SITE 187
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_03124"
FT SITE 261..262
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
SQ SEQUENCE 481 AA; 49837 MW; BAE9108161B38301 CRC64;
MHTCAPPHHF SSLKFPELHG SSKLNNLQVL RSFGLSKRSF KVFAVAASSS SSMSEASNYI
PAAPIFLPEG PWQQIPGGVT AAKGFKAAGI YGGLRAKGEK PDLALVTCDV DATAAGAFTT
NMVAAAPVLY CKNALDISKT ARAVLINAGQ ANAATGDAGY QDVLESVGAL AMLLKLKPEE
VLIESTGIIG QRIKKGALLN SLPKLVNSLS PSIEGAGSAA VAITTTDLVS KSVAIESQVG
GTNIKVGGMA KGSGMIHPNM ATMLGVITTD ALVNSDVWRK MVQISVNRSF NQITVDGDTS
TNDTVIALAS GLSGSISISN INCHEAMQLQ ACLDAVMQGL AKSIAWDGEG ATCLIEVTVT
GAESEAKAAK IARAVASSSL VKAAVYGRDP NWGRIAAAAG YAGIPFHQNN LRIMLGDILL
MDNGQPLSFD RSAASNYLRK AGEIHGTVGI YISVGDGPGS GQAWGCDLSY DYVKINAEYT
T
