ID   E6VPN1_RHOPX            Unreviewed;       907 AA.
AC   E6VPN1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=GCN5-related N-acetyltransferase {ECO:0000313|EMBL:ADU46010.1};
GN   OrderedLocusNames=Rpdx1_4459 {ECO:0000313|EMBL:ADU46010.1};
OS   Rhodopseudomonas palustris (strain DX-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=652103 {ECO:0000313|EMBL:ADU46010.1, ECO:0000313|Proteomes:UP000001402};
RN   [1] {ECO:0000313|Proteomes:UP000001402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DX-1 {ECO:0000313|Proteomes:UP000001402};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Misra M., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Logan B., Oda Y., Harwood C.,
RA   Woyke T.;
RT   "Complete sequence of Rhodopseudomonas palustris DX-1.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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; CP002418; ADU46010.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6VPN1; -.
DR   STRING; 652103.Rpdx1_4459; -.
DR   KEGG; rpx:Rpdx1_4459; -.
DR   eggNOG; COG0045; Bacteria.
DR   eggNOG; COG1042; Bacteria.
DR   eggNOG; COG1670; Bacteria.
DR   HOGENOM; CLU_007415_0_2_5; -.
DR   OrthoDB; 9807426at2; -.
DR   BioCyc; RPAL652103:RPDX1_RS22035-MONOMER; -.
DR   Proteomes; UP000001402; Chromosome.
DR   GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR043938; Ligase_CoA_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032875; Succ_CoA_lig_flav_dom.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR43334; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   PANTHER; PTHR43334:SF1; ACETATE--COA LIGASE [ADP-FORMING]; 1.
DR   Pfam; PF13302; Acetyltransf_3; 1.
DR   Pfam; PF13549; ATP-grasp_5; 1.
DR   Pfam; PF13380; CoA_binding_2; 1.
DR   Pfam; PF19045; Ligase_CoA_2; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
KW   Transferase {ECO:0000313|EMBL:ADU46010.1};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          743..899
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   907 AA;  97815 MW;  39F1AED6C7126B50 CRC64;
     MSTYRLSTLL SPSAVAVVGA SPRPASLGRA ILTNLREAGF KGAIGVVNPR YPEIGGFKTV
     DSLARLSFVP DLIVITAPPR SVAKVVAEAG ELGVAGAIII SSEMGRGKGS YAEAANRAAR
     KSGIRLIGPN CLGIMIPGAN LNASFAAHMP RRGNLALISQ SGAIAAGMVD WAAVKEIGFS
     GIVSIGDQLD VDIADMLDFY AADLETRAIL LYIEAVTDAR KFMSAARAAA RVKPVVVVKS
     GRMAHGAKAA ATHTGAFAGA DAVYEAAFRR AGMLRVYDLR ELFDCAETLG RVSAPRGKRV
     AILTNGGGIG ILAVDRLVEL GGEPATLSAD LHKKLDAILP TSWSGFNPID ITGDADAERY
     SATLSMLLAD PDNDAVLVMN VQTAVASPRD IAREVIRVVG EERVRRTLFK PVFAVWVGAE
     EAVTHAFDAA SIPNYPTEDD AVRSIMNMVR YREAGQLLTE VPPSLPKDFD PDTESARAIV
     EKALREKRSW LDPLEISGLF AAYQIPMIPT LAATNAEEAV SWASSFLSQG VTVVVKVLSR
     DIPHKSDIGG VVLNLTSVEA VRVAVDEILA RAARLRPDAR LDGVMVQPMI LRPKARELTI
     GIADDPTFGP VIAFGQGGTG VELIDDRSLA LPPLDLPLAE SLIGRTRVSK LLGAYRDVPE
     VKRSAVALTL VKLSQMAADL PEIRELDVNP LLADENGVVA IDARVVVREA ERKFAGRGNT
     HFAVKPYPTE WERHLIVKDG WRVLARPIRP DDEPAIHEFL KHVTPEDLRL RFFAAMKEFS
     HAFIARLSQI DYARAMAFVA FDEITGEMLG VVRIHSDSIY ESGEYAILLR SDLKGKGLGW
     TLMKLIIEYA RSEGLHYVCG QVLRENTAML RMCRDLGFES KTDPSEPDIL NVRLPLTEEA
     ARAAKSA
//