位置:首页 > 蛋白库 > ARGA_PSEPG
ARGA_PSEPG
ID   ARGA_PSEPG              Reviewed;         432 AA.
AC   B0KP70;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Amino-acid acetyltransferase {ECO:0000255|HAMAP-Rule:MF_01105};
DE            EC=2.3.1.1 {ECO:0000255|HAMAP-Rule:MF_01105};
DE   AltName: Full=N-acetylglutamate synthase {ECO:0000255|HAMAP-Rule:MF_01105};
DE            Short=AGS {ECO:0000255|HAMAP-Rule:MF_01105};
DE            Short=NAGS {ECO:0000255|HAMAP-Rule:MF_01105};
GN   Name=argA {ECO:0000255|HAMAP-Rule:MF_01105};
GN   OrderedLocusNames=PputGB1_5245;
OS   Pseudomonas putida (strain GB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=76869;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT   "Complete sequence of Pseudomonas putida GB-1.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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_01105};
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_01105}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01105}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. ArgA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01105}.
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; CP000926; ABZ01128.1; -; Genomic_DNA.
DR   RefSeq; WP_012274739.1; NC_010322.1.
DR   AlphaFoldDB; B0KP70; -.
DR   SMR; B0KP70; -.
DR   STRING; 76869.PputGB1_5245; -.
DR   EnsemblBacteria; ABZ01128; ABZ01128; PputGB1_5245.
DR   KEGG; ppg:PputGB1_5245; -.
DR   eggNOG; COG0548; Bacteria.
DR   eggNOG; COG1246; Bacteria.
DR   HOGENOM; CLU_024773_0_0_6; -.
DR   OMA; KRKYNWD; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000002157; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-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; cd04237; AAK_NAGS-ABP; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   HAMAP; MF_01105; N_acetyl_glu_synth; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR033719; NAGS_kin.
DR   InterPro; IPR010167; NH2A_AcTrfase.
DR   PANTHER; PTHR30602; PTHR30602; 2.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   PIRSF; PIRSF000423; ArgA; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR01890; N-Ac-Glu-synth; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW   Transferase.
FT   CHAIN           1..432
FT                   /note="Amino-acid acetyltransferase"
FT                   /id="PRO_1000084820"
FT   DOMAIN          286..425
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01105"
SQ   SEQUENCE   432 AA;  47399 MW;  8605EAC52A88EDDC CRC64;
     MPDYVNWLRH ASPYINAHRD CTFVVMLPGD GVEHPNFGNI VHDLVLLHSL GVRLVLVHGS
     RPQIESRLAD RGLTPHYHRG MRITDAATLD CVIDAVGALR LAIEARLSMD IAASPMQGSR
     LRVASGNLVT ARPIGVLEGV DYHHTGEVRR VDRKGISRLL DERSIVLLSP LGYSPTGEIF
     NLACEDVATR AAIELGADKL LLFGAEPGLL DADGKLVREL RPQQVAPHLQ RLGSDYQGEL
     LDAAAEACKG GVARSHIVSY AEDGALLTEL FTRGGGGTLV SQEQFEVVRE ASIEDVGGLL
     ELISPLEEQG ILVRRSREVL EREIEQFSVV EREGMIIACA ALYPIADSEA GELACLAVNP
     EYRHGGRGDE LLERIESRAR QMGLNTLFVL TTRTAHWFRE RGFAPSGVER LPAARASLYN
     YQRNSKIFEK AL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024