(data stored in SCRATCH zone)

SWISSPROT: ARGJ_LACTC

ID   ARGJ_LACTC              Reviewed;         441 AA.
AC   C5DCN3;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   16-JAN-2019, entry version 57.
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ, mitochondrial {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   OrderedLocusNames=KLTH0B04488g;
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284;
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- FUNCTION: Catalyzes two activities which are involved in the
CC       cyclic version of arginine biosynthesis: the synthesis of
CC       acetylglutamate from glutamate and acetyl-CoA, and of ornithine by
CC       transacetylation between acetylornithine and glutamate.
CC       {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;
CC         EC=2.3.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_03124};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-
CC         glutamate; Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:44337, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288; EC=2.3.1.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03124};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-
CC       acetyl-L-ornithine (cyclic): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_03124}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
CC       acetyl-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.
CC       {ECO:0000255|HAMAP-Rule:MF_03124}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC       Rule:MF_03124}.
CC   -!- PTM: The alpha and beta chains are autoproteolytically processed
CC       from a single precursor protein within the mitochondrion.
CC       {ECO:0000255|HAMAP-Rule:MF_03124}.
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-
CC       terminal transit peptide but none has been predicted.
CC       {ECO:0000255|HAMAP-Rule:MF_03124}.
CC   -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000255|HAMAP-
CC       Rule:MF_03124}.
DR   EMBL; CU928166; CAR21544.1; -; Genomic_DNA.
DR   RefSeq; XP_002551982.1; XM_002551936.1.
DR   SMR; C5DCN3; -.
DR   STRING; 381046.XP_002551982.1; -.
DR   MEROPS; T05.001; -.
DR   EnsemblFungi; CAR21544; CAR21544; KLTH0B04488g.
DR   GeneID; 8290819; -.
DR   KEGG; lth:KLTH0B04488g; -.
DR   HOGENOM; HOG000022798; -.
DR   InParanoid; C5DCN3; -.
DR   KO; K00620; -.
DR   OMA; GMIAPNM; -.
DR   OrthoDB; 934513at2759; -.
DR   UniPathway; UPA00068; UER00106.
DR   UniPathway; UPA00068; UER00111.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0005759; C:mitochondrial matrix; 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; 3.60.70.12; -; 1.
DR   HAMAP; MF_01106; ArgJ; 1.
DR   InterPro; IPR002813; Arg_biosynth_ArgJ.
DR   InterPro; IPR016117; ArgJ-like_dom_sf.
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;
DR   PRODOM; C5DCN3.
DR   SWISS-2DPAGE; C5DCN3.
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis;
KW   Autocatalytic cleavage; Complete proteome; Mitochondrion;
KW   Multifunctional enzyme; Reference proteome; Transferase.
FT   CHAIN         1    214       Arginine biosynthesis bifunctional
FT                                protein ArgJ alpha chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_03124}.
FT                                /FTId=PRO_0000398058.
FT   CHAIN       215    441       Arginine biosynthesis bifunctional
FT                                protein ArgJ beta chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_03124}.
FT                                /FTId=PRO_0000398059.
FT   ACT_SITE    215    215       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   BINDING     177    177       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   BINDING     204    204       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   BINDING     215    215       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   BINDING     301    301       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   BINDING     436    436       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   BINDING     441    441       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   SITE        136    136       Involved in the stabilization of negative
FT                                charge on the oxyanion by the formation
FT                                of the oxyanion hole. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   SITE        137    137       Involved in the stabilization of negative
FT                                charge on the oxyanion by the formation
FT                                of the oxyanion hole. {ECO:0000255|HAMAP-
FT                                Rule:MF_03124}.
FT   SITE        214    215       Cleavage; by autolysis.
FT                                {ECO:0000255|HAMAP-Rule:MF_03124}.
SQ   SEQUENCE   441 AA;  47232 MW;  D6A3DFFFBDFBB26B CRC64;
     MRVSSALLQK AAKTVDKYSL YVPKSGVFPK GFKVASLASG VKKNGNRDLG IILNTNKSRP
     SNAAAVFTTN RFKAAPVLVS KQVLDGSSGE GVNAIVANSG CANAVTGELG MQDAQKVAGQ
     VNAHIGKENS TLVMSTGVIG QRLQMDKISK GINTLFDQKQ FGSDFNSWLN LAKSICTTDT
     FPKLISSKFQ LSDGTEYTLT GISKGAGMIC PNMATLLGFI VTDLPIKAST LQAMLTAAVN
     RSFNCISVDG DMSTNDTICM LANGAVDTFV IDEASPDFEQ VKSQVTEFAK QLAQLVVRDG
     EGATKFVTVN VKNSANFKDA RIIAETISNS MLVKSALYGQ DANWGRILCA IGYSKLENLA
     SLDESKINVS FIATDNSSPR ELKLIANGVP QFDIDENRAS EILALPDLEI LVDMGTGSEE
     CQFWTCDLSH EYVTINGDYR S
//

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