GenomeNet

Database: UniProt
Entry: A0A151U4A6_CAJCA
LinkDB: A0A151U4A6_CAJCA
Original site: A0A151U4A6_CAJCA 
ID   A0A151U4A6_CAJCA        Unreviewed;       442 AA.
AC   A0A151U4A6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   31-JUL-2019, entry version 28.
DE   RecName: Full=Arginine biosynthesis bifunctional protein ArgJ, chloroplastic {ECO:0000256|HAMAP-Rule:MF_03124};
DE   Includes:
DE     RecName: Full=Glutamate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03124};
DE              Short=GAT {ECO:0000256|HAMAP-Rule:MF_03124};
DE              EC=2.3.1.35 {ECO:0000256|HAMAP-Rule:MF_03124};
DE     AltName: Full=Ornithine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03124};
DE              Short=OATase {ECO:0000256|HAMAP-Rule:MF_03124};
DE     AltName: Full=Ornithine transacetylase {ECO:0000256|HAMAP-Rule:MF_03124};
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03124};
DE              EC=2.3.1.1 {ECO:0000256|HAMAP-Rule:MF_03124};
DE     AltName: Full=N-acetylglutamate synthase {ECO:0000256|HAMAP-Rule:MF_03124};
DE              Short=AGS {ECO:0000256|HAMAP-Rule:MF_03124};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000256|HAMAP-Rule:MF_03124};
DE   Contains:
DE     RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000256|HAMAP-Rule:MF_03124};
GN   ORFNames=KK1_006779 {ECO:0000313|EMBL:KYP74111.1};
OS   Cajanus cajan (Pigeon pea) (Cajanus indicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
OC   50 kb inversion clade; NPAAA clade; indigoferoid/millettioid clade;
OC   Phaseoleae; Cajanus.
OX   NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP74111.1, ECO:0000313|Proteomes:UP000075243};
RN   [1] {ECO:0000313|EMBL:KYP74111.1, ECO:0000313|Proteomes:UP000075243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX   PubMed=22057054; DOI=10.1038/nbt.2022;
RA   Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K.,
RA   Schlueter J.A., Donoghue M.T., Azam S., Fan G., Whaley A.M.,
RA   Farmer A.D., Sheridan J., Iwata A., Tuteja R., Penmetsa R.V., Wu W.,
RA   Upadhyaya H.D., Yang S.P., Shah T., Saxena K.B., Michael T.,
RA   McCombie W.R., Yang B., Zhang G., Yang H., Wang J., Spillane C.,
RA   Cook D.R., May G.D., Xu X., Jackson S.A.;
RT   "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume
RT   crop of resource-poor farmers.";
RL   Nat. Biotechnol. 30:83-89(2012).
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:0000256|HAMAP-Rule:MF_03124, ECO:0000256|SAAS:SAAS01092298}.
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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-
CC       Rule:MF_03124}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000256|HAMAP-Rule:MF_03124, ECO:0000256|SAAS:SAAS01092300}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_03124}.
CC   -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000256|HAMAP-
CC       Rule:MF_03124}.
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; CM003604; KYP74111.1; -; Genomic_DNA.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000075243; Chromosome 2.
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; 1.
DR   Pfam; PF01960; ArgJ; 1.
DR   SUPFAM; SSF56266; SSF56266; 1.
DR   TIGRFAMs; TIGR00120; ArgJ; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Chloroplast {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Complete proteome {ECO:0000313|Proteomes:UP000075243};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Plastid {ECO:0000256|HAMAP-Rule:MF_03124};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075243};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03124}.
FT   ACT_SITE    225    225       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     188    188       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     214    214       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     225    225       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     312    312       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     437    437       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   BINDING     442    442       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03124}.
FT   SITE        149    149       Involved in the stabilization of negative
FT                                charge on the oxyanion by the formation
FT                                of the oxyanion hole. {ECO:0000256|HAMAP-
FT                                Rule:MF_03124}.
FT   SITE        150    150       Involved in the stabilization of negative
FT                                charge on the oxyanion by the formation
FT                                of the oxyanion hole. {ECO:0000256|HAMAP-
FT                                Rule:MF_03124}.
FT   SITE        224    225       Cleavage; by autolysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_03124}.
SQ   SEQUENCE   442 AA;  45925 MW;  26797038D8DE6ECC CRC64;
     MFGLASSAPH FRIRAVSTTQ NHIPPAPIFL PQGPWNQIPG GVTAAEGFKA AGIYGGLRAK
     GEKPDLALVT CDVDAVSAGS FTTNVVAAAP VLYCKKTLDI SNTARAVLIN AGQANAATGK
     EGYQDVIECV ESLAKLQKVK PEEILVESTG VIGQRIKKGK LLNSLPTLVS SLSSSVEGAD
     SAAVAITTTD LVSKSVAIES LVGGTKVRIG GMAKGSGMIH PNMATMLGVI TTDARVTSDV
     WRKMVQVAVN RSFNQITVYG DTSTNDTVIA LASGLSGIGC ISSLDNDEAI QLQACLDAVM
     QGLAKSIAWD GEGATCLVEV SVTGANSEAE AAKVARSVAS SSLAAIYGRD PNWGRIAAAA
     GYSGVSFHQD SLRVELGDIL LMDGGEPQLF DRNAASSYLR KAGETHDTVR IQISVGNGPG
     RGQAWGCDLS YDYVKINAEY TT
//
DBGET integrated database retrieval system