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
//