ID A0A1I1WBW0_9BURK Unreviewed; 897 AA.
AC A0A1I1WBW0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Acetyltransferase {ECO:0000313|EMBL:SFD92511.1};
GN ORFNames=SAMN04489710_10923 {ECO:0000313|EMBL:SFD92511.1};
OS Paracidovorax konjaci.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Paracidovorax.
OX NCBI_TaxID=32040 {ECO:0000313|EMBL:SFD92511.1, ECO:0000313|Proteomes:UP000199517};
RN [1] {ECO:0000313|EMBL:SFD92511.1, ECO:0000313|Proteomes:UP000199517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7481 {ECO:0000313|EMBL:SFD92511.1,
RC ECO:0000313|Proteomes:UP000199517};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOMQ01000009; SFD92511.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1WBW0; -.
DR STRING; 32040.SAMN04489710_10923; -.
DR OrthoDB; 9807426at2; -.
DR Proteomes; UP000199517; 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 Transferase {ECO:0000313|EMBL:SFD92511.1}.
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; 96348 MW; 2A46EDEB12DFBEE2 CRC64;
MIEKHYLTPL FAPSSIAVLA GRADAPETLT PAARALHEAL RAQRFTGTLQ FLDIHTSGTL
ADLAQTRADL AVIAQQPQDT AAALEVAGRI GCRAALVLSQ GLDADTALRL KKIARREGMH
LLGPNSLGLQ RPHLQLNASA AGPLAREGSL ALVCQSGALT ASILDWAHKN AVGFSTVVSL
GPNTDVDISQ VLDFLANDGR TQSIVVYMEG IGSARRFMSA LRSAANAKPV VVLKAGRKPA
GNEAAQTHSG TIVGSDDVFD AALRRAGAVR VRSFVELFSA AKCLASRYRP VGKRLALVTN
GGGPGVLAAD WVNEILLEMG RLSADAAQAL APQLPPLASL ADLIDLSEEA GPAHYRAAIE
AAERDRQIDG VLAIHSPKAG TDAVDVARAL AEAKRLMGKP LLACWMGDAT VGPAREVLRA
AAIPSFRTPE AAVGAFGNIA SFYQNQQLLQ QTPPPLSALS KPDIEGARLL IESVLAERRS
VLTEMESKTL LAAFQVPVTK TLLARSAHEA MMIATQLGFP VALKIDSPDI SHKSDVGGVA
LDIHSGTAAR DAYTDMVQRV ARLQPGARIN GVTVQKMARA RRGREICIGL VTDDPFGPVI
TFGAGGTMIE LIDDRAMELP PLNQFLARRL IERSRVAETL GEWRGASAVD RDALEQTLLR
VSEMVCALPQ LREMDINPLI VDAGGVVAVD ARIAVRDTAQ AASGRSEGYG HLAILPYPAR
YEQTWPMRGG GEFLVRPVRP DDAQMLQRLV KELSPESRYF RYISQIAELP APMLARFTLI
DYDREMALVA VHRERSAGED GEIRNTERIV GVSRYVTNPD QTSCEFALVV ADDFNGRGLG
SRLMLSIMEA ARDKGLTEIQ GLVLAQNPSM LKLMRRLGFE VRAYPDDPDF KLVAHQL
//
