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Database: UniProt
Entry: I3U9N2_ADVKW
LinkDB: I3U9N2_ADVKW
Original site: I3U9N2_ADVKW 
ID   I3U9N2_ADVKW            Unreviewed;       822 AA.
AC   I3U9N2;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Acetyltransferase {ECO:0000313|EMBL:AFK61720.1};
GN   OrderedLocusNames=TKWG_06355 {ECO:0000313|EMBL:AFK61720.1};
OS   Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS   (Tetrathiobacter kashmirensis).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae.
OX   NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK61720.1, ECO:0000313|Proteomes:UP000005267};
RN   [1] {ECO:0000313|EMBL:AFK61720.1, ECO:0000313|Proteomes:UP000005267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17095 / LMG 22695 / WT001
RC   {ECO:0000313|Proteomes:UP000005267};
RX   PubMed=21914874; DOI=10.1128/JB.05781-11;
RA   Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT   "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT   Tetrathiobacter kashmirensis.";
RL   J. Bacteriol. 193:5553-5554(2011).
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DR   EMBL; CP003555; AFK61720.1; -; Genomic_DNA.
DR   RefSeq; WP_014749811.1; NC_017964.1.
DR   AlphaFoldDB; I3U9N2; -.
DR   STRING; 1036672.TKWG_06355; -.
DR   KEGG; aka:TKWG_06355; -.
DR   HOGENOM; CLU_007415_0_2_4; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000005267; Chromosome.
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; PF13302; Acetyltransf_3; 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:AFK61720.1}.
FT   DOMAIN          669..819
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   822 AA;  91189 MW;  334682A7CE1A231A CRC64;
     MLRHRLAAFF EPRSLCVIAD TELAVFAQVP AYLKASTDLL PLPDDLSSAQ QQLRHWTMTP
     GRDLAVICVR SGLLGAVLQQ MAVAPPRAVL LLPGQVVDQA PQDTRDLIQD WCREHGVMLL
     GPRAFGIYRP HLNLNLSLAQ MQPRAGRIAV ISQSRMLLRS IIDWAEDVNL GLSAAVSLGE
     VTDVDLPELV EYLATDPRTD SIALYLDKLT SGRELISALR AASSVKPVIV LRAGRADPDL
     SGSDVVLDAA LRRAGAIRVN YFVELFAAIK AMSYARRPRG GKIAMLANGR ASAQLVQDAI
     PADSSMSMAP LTQGTVKCLS EIFGVSTLVD NPVIPYVPLT PEALIDGLQC LIADSQVDAV
     MVILAPDEFC DMQQVVKALA AFAPGAKKPI VTCLLGEAKM RPLRRLLDQA GMPAFRTPET
     ALSAVLSLTS YHYNQQLLQQ TRYVHSGQRP AELEQARAIL EAAGSVAAGE LTRQQCIDLV
     ECFHPDVRWE RDEEDERFSS LDDVPSVMIR VRCDPVFGPW IWFGEGGHMV RFSASDRGVD
     LPPLNLNLAG KLIERSRVWR QELQSYVEPQ ILRKLQGLLE TISEMVSELP AIEAMELDPI
     ILGYRDLHVR EIRIRLAKSL PALIPQKTGF SHMAIYPYPT HLVQNRVFTD GSPWILRPIR
     PEDADALQEF IRGLSEKSRY MRFVSMMREL TPKMLTRYTY VDYHRELALV ATTQIPNPAN
     RGLPQEIIIG LAHYLRNADG VGAEYALVIS DQWQKRGLGS SLMEALIMAA RQQQLSYLEG
     VVLSSNRPML HLMTSLGFIN EEDAEDPSMR RVWLPLTMAE SA
//
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