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Database: UniProt
Entry: A0A158FVJ8_9BURK
LinkDB: A0A158FVJ8_9BURK
Original site: A0A158FVJ8_9BURK 
ID   A0A158FVJ8_9BURK        Unreviewed;       720 AA.
AC   A0A158FVJ8;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=N-acetyltransferase GCN5 {ECO:0000313|EMBL:SAL23379.1};
GN   ORFNames=AWB68_00965 {ECO:0000313|EMBL:SAL23379.1};
OS   Caballeronia choica.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=326476 {ECO:0000313|EMBL:SAL23379.1, ECO:0000313|Proteomes:UP000054770};
RN   [1] {ECO:0000313|Proteomes:UP000054770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Peeters C.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FCON02000007; SAL23379.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158FVJ8; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000054770; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR003781; CoA-bd.
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; PF13549; ATP-grasp_5; 1.
DR   Pfam; PF13380; CoA_binding_2; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   SMART; SM00881; CoA_binding; 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; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Transferase {ECO:0000313|EMBL:SAL23379.1}.
FT   DOMAIN          502..538
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   720 AA;  74856 MW;  6EC683135C756585 CRC64;
     MSVFPSLERL VEPRSVVIVG ASSREGSQGH RLVMNVLEHS RFAGDVHLVN PSGLSICGRP
     CWPSIDAVPA GDIDVALVIV NASRVMEALR QCAARGIPFA IVMSSGFAEA DEAGKALEAE
     IADLCRATGL RVYGPNCPGF VNVRDRIGLT FSPAFKDDLN GGAIGLATQG GGLGRNVLQS
     LSYGEGVGLW FSAGNEVDLG VPDFIAHMAT DPRISVIAVL MEGIKDGRKL IDALKLAREN
     AKPVVILKVG RSELGVRAAQ SHTASIAGSA AVNSAVFRQY GAIEVDDLSE LAAVSKLCLR
     ARTLGGDGVC VLSFSGGACA LAADAVGAAQ LPMASLHEQT TAALREVLPA FASVANPVDT
     TADIMRDSAM TSACLRTLCE EPNVGAVLFP IPMDYGDITG AMASAIVEAS RTSKAVVVPV
     WMSRRMGKGF QMLESNGLQP FLSVTEAVRA LKKVHDWRAG QISACAAQTP AAHGDTGVSG
     GAEVGQGQMV GATPALTEVD AKRLLGRHGI VVPSGELTMS AAAAAETATR IGFPCVMKVV
     SPDIAHKTEA GGVRLNLETA ADARTAYDEI VANAGRYRPD AIVEGVLVER MLPPGGREML
     VGVHRDEAFG PVLTVGLGGI LVEVLKDVSH RVIPVDHADA RRMIAELRHS DLLGAVRGQP
     PADVEALAAL LVQVSEFVER AHGAIDQLDI NPVWVGALGE GAIALDALMV LAQGADANAL
//
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