ID A0A080MAU5_9PROT Unreviewed; 907 AA.
AC A0A080MAU5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 03-MAY-2023, entry version 23.
DE SubName: Full=Acetyltransferase Pat {ECO:0000313|EMBL:KFB74264.1};
DE EC=2.3.1.- {ECO:0000313|EMBL:KFB74264.1};
GN ORFNames=AW09_000447 {ECO:0000313|EMBL:KFB74264.1};
OS Candidatus Accumulibacter phosphatis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=327160 {ECO:0000313|EMBL:KFB74264.1, ECO:0000313|Proteomes:UP000020077};
RN [1] {ECO:0000313|EMBL:KFB74264.1, ECO:0000313|Proteomes:UP000020077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA-91 {ECO:0000313|Proteomes:UP000020077};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) 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:KFB74264.1}.
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DR EMBL; JDVG02000071; KFB74264.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080MAU5; -.
DR Proteomes; UP000020077; 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 Acyltransferase {ECO:0000313|EMBL:KFB74264.1};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Transferase {ECO:0000313|EMBL:KFB74264.1}.
FT DOMAIN 508..544
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 749..906
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 907 AA; 99592 MW; 4922FA8E7EFB9B82 CRC64;
MAPLEQAAKI LMLEHHYLTT LFEPKSVAVI GASDRENSVG NVLFKNILDS GYKGRLYPIN
TAHESIQGVQ AYKSIEEISA RVELAVVVTR PQTVPKIIEQ CGRSGVKNAI VITSGFAETG
HSGAALERKM MEIARSYGVR LLGPNCLGII RPSLGLNATF AHVYANVGNL ALVSQSGAIC
SAVLDWATSN RVGFSSVISL GGTADVDFGE ILDYLIYDNL THYILLYVEG IRDARRFMSA
LRSAARIKPI VLLKAGRHAG GLAAVETHSG MPGGSDIVFE AAVRRAGVVR VKNIGQLFYA
AKALASKFRP QGKRLAIITN GGGPGAMAAD RAGDLEIPLA ELSASTIQKL NSKMPPTWSQ
RNPIDIEGDA TPKRYHEAIL AVAEDDTVDG VLVMLSPQAM TKPMEVAKAV IEVDLLTAKP
ILTCWMGEEQ VLEARMLLEE SGIPSFRMPE TAVELYYHIS TYYWNQKLLL QTPAPLSKHS
RPETEGARML VEAVLHERRK VLSEMESKAI LRAFRIPVAQ TMVAHTPTES LLLAEQIGFP
IAMKIDSPDI IHKSEVGGVR LNISNAPAAR NAYHDILETV KKRHPTARIN GVSIEPYLAR
PNGRELMIGV SRDPIFGPII TFGAGGTEVE VFSDRAVALP PLNRFLARDL IASTRASKLL
GEFRNMPAVN LEALEDVLLH VSQMICELPW LQELDLNPLI VDENGGIAAD ARIVIDYAAP
SGDRYAHMAI HPYPAHLIQE WELPDGRTVT IRPIRPEDAE REQQFVIGLS DESKYYRFMD
TIRELTQTML VRFTQIDYDR EMALVATLPD ADGKELQIGV ARYVTNPDGE SVEFALAVAD
DWQKHGVGRK LMSALIDCAR VKGYRTIVGD VLSMNTKMFN LMTRLGFTIH PHPDDPAVKR
VIKPLNN
//
