ID A0A3S0VML8_9GAMM Unreviewed; 893 AA.
AC A0A3S0VML8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 03-MAY-2023, entry version 14.
DE SubName: Full=Bifunctional acyl-CoA synthetase/GNAT family N-acetyltransferase {ECO:0000313|EMBL:RUQ84503.1};
GN ORFNames=EKM59_08640 {ECO:0000313|EMBL:RUQ84503.1};
OS Legionella septentrionalis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=2498109 {ECO:0000313|EMBL:RUQ84503.1, ECO:0000313|Proteomes:UP000288012};
RN [1] {ECO:0000313|EMBL:RUQ84503.1, ECO:0000313|Proteomes:UP000288012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=km714 {ECO:0000313|Proteomes:UP000288012};
RA Wu H.;
RT "Legionella sp,whole genome shotgun sequence.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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:RUQ84503.1}.
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DR EMBL; RZGR01000026; RUQ84503.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0VML8; -.
DR Proteomes; UP000288012; Unassembled WGS sequence.
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:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR011761; ATP-grasp.
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; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000288012};
KW Transferase {ECO:0000313|EMBL:RUQ84503.1}.
FT DOMAIN 496..532
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 737..893
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 893 AA; 98123 MW; DA1C461F38F850CA CRC64;
MSAHYLDKFF NPSAIAVIGA SSRTNSVGMK VFANLLGANF AGQLYPVNPK HTKIQGYHAF
PNVLDIPHAI DLAIITTPAQ TVPIILDQCG KKNIKAAVII SAGFSESGNE GKEWEQSALN
LAHHYNMRLI GPNCLGLMRP ACGLNATFNN TFAMSGSIAL VSQSGAICAA ILDWAIDKRI
GLSAMVSLGN AVDLDFGEIL DFLAVDAETK SILLYIEGIH NARRFMSGLR AAARMKPVIV
IKGGRLAQGS RAAYSHTGAL VGDDDAFDAA LRQAGAVRVM TIKQLFSAAE ILSSNYRTQG
NRLAIITNGG GAGVMAADRA SELNIPLAPL NEHTITQLNQ ILPRAWSHQN PIDILGDATP
ERYHHTVKIC AKDENIDGLL NILIPVAMSN PLKVAKQLLL DAKESTKPII ACWMGEHHVK
SSWELFAQHN IPCFSTPEEA IEAFSYLAEY HHNQQLLLQV PEPRLHRPKH DVQGARLIIE
SVLGERRNLL STMESKAILK AFAIPITSAI ATHSANEALI AAETLQFPVV MKINSPDITH
KQDAGGVKLN IEHAGAVRDT YHQLIENAKQ YRPDANITGV TVEKMYKDPN NREVMIGVVR
DKVFGPVITF GAGGTFVEII RDRAVALPPL NPYLANHLID RTRIAKLLGK FRNMLPANTD
ALLNVLLNVS AMVCELPYIR EMDINPLLVN DKEAIAVDVR IVVDAPVTST VPYQHMAICP
YPSHLSSTWQ MTDSTHITIR PIRPEDAQIE QEFVKNLSPQ SRYFRFMEHL QELTLSTLIR
FTQIDYDREM AFIATCKKID KEIAIGVARY YMANDAGDTC EFGLVIADAW QNKGLGTRLM
KVLQDAAKHR GVKMMRGEIL AENKPMLDLV ENLGFTVMSV ADPKIKIASK QLT
//
