位置:首页 > 蛋白库 > ARGA_HAEDU
ARGA_HAEDU
ID   ARGA_HAEDU              Reviewed;         437 AA.
AC   Q7VLN8;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 113.
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}; OrderedLocusNames=HD_1384;
OS   Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=233412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=35000HP / ATCC 700724;
RA   Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA   Nguyen D., Wang J., Forst C., Hood L.;
RT   "The complete genome sequence of Haemophilus ducreyi.";
RL   Submitted (JUN-2003) 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   -!- MISCELLANEOUS: In bacteria which possess the bifunctional enzyme
CC       ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), ArgA
CC       fulfills an anaplerotic role.
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; AE017143; AAP96197.1; -; Genomic_DNA.
DR   RefSeq; WP_010945246.1; NC_002940.2.
DR   AlphaFoldDB; Q7VLN8; -.
DR   SMR; Q7VLN8; -.
DR   STRING; 233412.HD_1384; -.
DR   PRIDE; Q7VLN8; -.
DR   EnsemblBacteria; AAP96197; AAP96197; HD_1384.
DR   KEGG; hdu:HD_1384; -.
DR   eggNOG; COG0548; Bacteria.
DR   eggNOG; COG1246; Bacteria.
DR   HOGENOM; CLU_024773_0_0_6; -.
DR   OMA; KRKYNWD; -.
DR   UniPathway; UPA00068; UER00106.
DR   Proteomes; UP000001022; 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   Reference proteome; Transferase.
FT   CHAIN           1..437
FT                   /note="Amino-acid acetyltransferase"
FT                   /id="PRO_0000186793"
FT   DOMAIN          289..437
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01105"
SQ   SEQUENCE   437 AA;  49314 MW;  12CE064EDBADD241 CRC64;
     MRNTELIEWF RQSAPYVNMH RHKTFVIMLD GNAIAHPNFI NITNDISLLH SLGIKLVIVF
     GARCQIENLL KQNNISSSYH HNIRVTDSNM LEIIKQAVGG LHYDIFSRLS LRLPHSPVLN
     VVSSNAILAQ PLGVIDGVDY GLSGKIRRIN IEAIQQQLAQ NAIVVIGPIA PSVTGKMFNL
     AFEEIATQLA IKLKVDKLIA FCDRQGLLDE QGKVISDIHP REAKQHLKKF IQQGDYHHSA
     ARFLQAAIDV CHAGIKRSHL ISYQTDGSLL QELFSRDGVG TQLSEASSEC IRLATSFDIA
     GLLNLIRPLE DQGLLVKRSR EQLEMEISQY TIIERDGIVI ACAALIHYPA EKMAEMACVA
     VHPDYRDSAR GDILLEAIKR RAYKLNIEKL FVLTTQTIQW FQERGFVQIQ PTDLPVEKQR
     HYNYQRMSKV LMLALDN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024