ID A0A2U1C2J0_9BURK Unreviewed; 897 AA.
AC A0A2U1C2J0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:PVY55130.1};
GN ORFNames=C8D04_0308 {ECO:0000313|EMBL:PVY55130.1};
OS Simplicispira sp. 125.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Simplicispira.
OX NCBI_TaxID=2135643 {ECO:0000313|EMBL:PVY55130.1, ECO:0000313|Proteomes:UP000245599};
RN [1] {ECO:0000313|EMBL:PVY55130.1, ECO:0000313|Proteomes:UP000245599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=125 {ECO:0000313|EMBL:PVY55130.1,
RC ECO:0000313|Proteomes:UP000245599};
RA Chistoserdova L.;
RT "Synthetic bacterial communities of pure cultures isolated from sediment of
RT Lake Washington, USA.";
RL Submitted (APR-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:PVY55130.1}.
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DR EMBL; QEKM01000001; PVY55130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1C2J0; -.
DR Proteomes; UP000245599; Unassembled WGS sequence.
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; IPR000182; GNAT_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; 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; 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:UP000245599};
KW Transferase {ECO:0000313|EMBL:PVY55130.1}.
FT DOMAIN 488..524
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 733..897
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 897 AA; 96493 MW; 0ED30877C1BD1BF4 CRC64;
MEKHYLTPLF SPETVAVFAG DCEDDAHLTS QAKALHEALR AQRYTGRLVF VDLQKTTGSL
ADLVQTRADL AVIALPAADV AAALEVAGRM ACRAAMIVSS GIGPDLATQL KKIAHREGMY
LLGPNSLGLQ RPALQLNASA AGPLARTGSL ALVSQSGALT ASILDWARNN AVGFSSVVSL
GPNTDIDIAQ VLDFLANDPQ THSIVVYMEG ITSARAFMSA LRSAANAKPV VVLKAGRKPA
GNEAAQTHSG TIVGSDDVFD AALRRAGAVR VRSFVALFSA AKCLASRYRP VGRRLAIVTN
GGGPGVLAAD WVNEIFLDLG KLSPESAAAL KPQLPELASL SDLIDVSEDA TAEHYRIAVE
AASKDRQIDG VLAIHSPKSG VDPSDVARVL AEVKRQMTKP LLTCWMGDAT VVPARGILLE
ASIPSFRTPE AAVGAFGNIA AFHQNQQLLQ QTPPPLSALA KPDIKGARLV IESVLAERRK
VLTEMESKTL LAAFHIPVTK TILARSAHEA MMIATQLGFP VALKIDSPDI SHKSDVQGVA
LNVIDGASAR DTYTDMVARV ARLQPHARIN GVTVQNMVRA RRGREVCIGL VTDDPFGPVI
TFGAGGTMIE LINDRAMELP PLNQFLARRL IERSRVAETL GEWRGATAAD HEALEQILLR
VSEMVCQLPQ LREMDINPII VDESGAVAVD ARIVIDHAPH SGNGSVGQYG HLAILPYPAR
YEQIWPLRGG GEYTVRPIRP DDAQMLQTLV QNLSPESRYF RFISSMAQLP PMMLARFTLI
DYDREMALVA IFKERKAGPD GEIVETERIV GVSRYITNPD HSSCEFALVV ADDFSGKGLG
SRLMLSIMDV ARDKGLAEIE GLVLANNPEM LKLMRNLGFS IKAYADDPEF KMVTHTL
//