ID A0A0S8CJ51_9CHLR Unreviewed; 902 AA.
AC A0A0S8CJ51;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 28-JUN-2023, entry version 21.
DE RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51186};
GN ORFNames=AMJ70_02895 {ECO:0000313|EMBL:KPK23671.1};
OS Dehalococcoidia bacterium SG8_51_3.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703394 {ECO:0000313|EMBL:KPK23671.1, ECO:0000313|Proteomes:UP000051285};
RN [1] {ECO:0000313|EMBL:KPK23671.1, ECO:0000313|Proteomes:UP000051285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_51_3 {ECO:0000313|EMBL:KPK23671.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK23671.1}.
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DR EMBL; LJTX01000040; KPK23671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CJ51; -.
DR PATRIC; fig|1703394.3.peg.1864; -.
DR Proteomes; UP000051285; 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: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; 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; PS51186; GNAT; 1.
PE 4: Predicted;
FT DOMAIN 24..183
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 902 AA; 98411 MW; 749CA25DCD10D326 CRC64;
MAVKKAAYPS KYETEVLLKD GSRILLRPIR QDDVERWLSF FQRQSEQTKY LRFQRDPGEM
GPEDALRFCT VDYKNTFALV GEVQREKRKE IIAIGRYYRL PNKRSARVAF AIEDAYHGKG
IGTRLIEWLA NAARDNGITA FEGDVLAENE RMMAVLRDYG FHIDSELKGG VYHVTITIAR
SRRVERKEAE RERLSTIASI RNVLSPRSVA VIGASRQPGS IGQLVFQNIM EGGFSGVVYP
VNPKADAIMA VKAYPSILDV PGEVDLAIII VPTQFVARVA DECGRKGVRA IIVITDGFRE
RGREGAAREE ELRGIALGHG MRLVGPNCMG IINADPEVRL NASFSRVFPP RGNIAFLSQS
GAMGLVILEY ANDLNMGISG FISVGNRADI SSNDLLQYWE DDPATRVILL YLESFGNPHK
FSRIARRVAA KKPIVVVKSG TTLVGSRAAS SHTGALATPE VVSDALFRQA GIIRVDSIEE
LFDVATLLSS QPPPEGKRLV IVTNGGGPGI LAADASEQHG LTLPELSSET AGKLGELIKR
DISVGNPLDL TGSVTPEEFE GSLRVLVEDD SVDAVLAVFV PAAVVDSTLV EDAIRRVSPL
YQRRKKPLLV CFMGQRGFKA RLGKAGSFVP CYPFPEDAVS ALAKAVEYRE LVKKPGGTVP
HIKGVKRERA RHIIETAMSR NKQRPFWLST KEIVALLDCY GIHTVETAVA GSADEAAALA
ARTSFPVVVK LNSSTITHKT DVGGVVLDLN SKNEVKEAFN DIKKKLAALG REPEMEGVTI
QRMISGGVEI IAGVTQDPTF GPLIMFGLGG VQAELLKDIV LRLHPLTEVD ASEMVSSIKM
ARLFEGFRGA PPSDIPAVQD LLLRLSAMVE DIPQVAELDF NPVKVMAKGE GYRVVDARIS
LK
//
