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Database: UniProt
Entry: H0F7L7_9BURK
LinkDB: H0F7L7_9BURK
Original site: H0F7L7_9BURK 
ID   H0F7L7_9BURK            Unreviewed;       805 AA.
AC   H0F7L7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=GNAT family acetyltransferase {ECO:0000313|EMBL:EHK65758.1};
GN   ORFNames=KYC_13823 {ECO:0000313|EMBL:EHK65758.1};
OS   Achromobacter arsenitoxydans SY8.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=477184 {ECO:0000313|EMBL:EHK65758.1, ECO:0000313|Proteomes:UP000003113};
RN   [1] {ECO:0000313|EMBL:EHK65758.1, ECO:0000313|Proteomes:UP000003113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY8 {ECO:0000313|EMBL:EHK65758.1,
RC   ECO:0000313|Proteomes:UP000003113};
RX   PubMed=22328747; DOI=10.1128/JB.06667-11;
RA   Li X., Hu Y., Gong J., Lin Y., Johnstone L., Rensing C., Wang G.;
RT   "Genome sequence of the highly efficient arsenite-oxidizing bacterium
RT   Achromobacter arsenitoxydans SY8.";
RL   J. Bacteriol. 194:1243-1244(2012).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHK65758.1}.
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DR   EMBL; AGUF01000048; EHK65758.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0F7L7; -.
DR   STRING; 477184.KYC_13823; -.
DR   PATRIC; fig|477184.5.peg.2740; -.
DR   eggNOG; COG1042; Bacteria.
DR   eggNOG; COG1670; Bacteria.
DR   Proteomes; UP000003113; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
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; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF13549; ATP-grasp_5; 1.
DR   Pfam; PF13607; Succ_CoA_lig; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
DR   PROSITE; PS51186; GNAT; 1.
PE   4: Predicted;
KW   Transferase {ECO:0000313|EMBL:EHK65758.1}.
FT   DOMAIN          657..805
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   805 AA;  87577 MW;  4F38B9AB40305AD3 CRC64;
     MFEPGSLVIV ADRPLPAATS LSPALKAKTT IVAAETGAAP ELPATLQGLA AGERPDLALV
     CVSPAVLPET LRRLSPLSPR AVILLPHELP DPYPRGTLAL CRAWAEENRC ELLGPRSFGA
     QRPHAGLNFS QHPVLARSGR VALVAQSRSI MAAVMDWAED VHIGFSTAVS LGDEAVVGLP
     KLLDYLASDP RTDSIVLYLE DVGPAREFMS TLRAAASIKP VIVLKAGRSD ADGADAIFDA
     ALRRAGAVRV RYFVQLFSAV KVLGYTRRPK GRRVALISNG SGPPQLAMDL IGPDAAVLRA
     DLAPATRRAL ADMLEPDAAT ANPVITYLPM TPDRIRAILD AVLDDAGVDG VLVLLAPDAL
     ADMPAVAREL AQIAPSAKKP VVTCFMGDAG MRPLRRMLDD AGTSAFRTPE SAADAFGVLA
     SHHYNQQLLL QTQPPEPASH VPDLAAAREI LARVRADCRR ELNTSEIRVL LALFYVPVRD
     LPADAPRIES ESRPMAIRVR RDPQFGPVIR FGAGGPDAVL SLADRGMDLP PLNGYLARQL
     IERSRLWRRV LAPRVGHMAA EALQQALVLV SELVSELPDI ESLDIDPLYA GETHLRAGGL
     RMTLTEQPGC ESPQTAGYPH MAIHPYPARL VQVRRFADGI PWVLRPIRPE DGEALQEFIR
     GLSERSRYMR FVSMMRELTP RMVSRYTQVD YHRELALVAA TQVPNPANRG HPREVLVGFA
     HYLRNPDGRG AEYALVIGDD WQRRGLGRQL MTALIDAARE QGLEYIDGLV LSTNRPMLSL
     MTSLGFTNDA DPEDPTMRRV WLNLS
//
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