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ARGJ_VITVI
ID   ARGJ_VITVI              Reviewed;         510 AA.
AC   A5AEC8;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=VITISV_037692;
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir;
RX   DOI=10.1371/journal.pone.0001326;
RA   Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA   Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA   Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA   Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA   Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA   Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA   Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA   Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA   Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA   Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT   "A high quality draft consensus sequence of the genome of a heterozygous
RT   grapevine variety.";
RL   PLoS ONE 2:E1326-E1326(2007).
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; AM424444; CAN77854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5AEC8; -.
DR   SMR; A5AEC8; -.
DR   MEROPS; T05.002; -.
DR   PRIDE; A5AEC8; -.
DR   UniPathway; UPA00068; UER00106.
DR   UniPathway; UPA00068; UER00111.
DR   ExpressionAtlas; A5AEC8; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; 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; 2.
DR   Pfam; PF01960; ArgJ; 2.
DR   SUPFAM; SSF56266; SSF56266; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW   Autocatalytic cleavage; Chloroplast; Multifunctional enzyme; Plastid;
KW   Transferase.
FT   CHAIN           1..259
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ
FT                   alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT                   /id="PRO_0000397992"
FT   CHAIN           260..510
FT                   /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT                   chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT                   /id="PRO_0000397993"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         359
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         505
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   BINDING         510
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
FT   SITE            184
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            185
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            259..260
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03124"
SQ   SEQUENCE   510 AA;  54114 MW;  C03E4302C49872BA CRC64;
     MFLCVPHYTS ITFPQLNDGR KVLRFGSYQR RGFRILAMSS SVSEASNYIT AAPIFLPDGP
     WKQIPGGVTA AKGFKAAGLY GGLRAKGEKP DLALVACDVD AISAGAFTTN VVAAAPVVYC
     KNALDMSKTA RAVLINAGQA NAATAKRPSN DYQGDAGYQD VIECANALAK LLQMRPEEVL
     IESTGVIGHR IKKDALLNSL PKLVSSLSSS TEGADSAAVA ITTTDLVSKS VAIESEVGGT
     NIRVGGMAKG SGMIHPNMAT MLGVRLCFLH VLFCKVVTTD ALVASDVWRK MVQIAVNRSF
     NQITVDGDTS TNDTVIALAS GLSGSTRISS LISHEAIQLQ ACLDAVMQGL AKSIAWDGEG
     ATCLIEGSSL VNAATIRIWR YRGHMAMPTG PLRIISLHLW YWAINHVELC FAAVYGRDPN
     WGRIACAAGY AGIPFQPNKL HISLGEILLM EGGQPLPFDR AAASNYLKKA GETHGTVGIH
     ISIGDGAGRG QAWGCDLSYD YVKINAEYTT
 
 
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