ID A0A0F7D0W2_SERFO Unreviewed; 883 AA.
AC A0A0F7D0W2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Protein acetyltransferase {ECO:0000313|EMBL:AKG67930.1};
GN ORFNames=WN53_01525 {ECO:0000313|EMBL:AKG67930.1};
OS Serratia fonticola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG67930.1, ECO:0000313|Proteomes:UP000034699};
RN [1] {ECO:0000313|EMBL:AKG67930.1, ECO:0000313|Proteomes:UP000034699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG67930.1,
RC ECO:0000313|Proteomes:UP000034699};
RA Chan K.-G., Ee R.;
RT "Complete Genome Sequencing of Serratia Fonticola DSM-4576.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP011254; AKG67930.1; -; Genomic_DNA.
DR RefSeq; WP_024484853.1; NZ_SUPV01000028.1.
DR AlphaFoldDB; A0A0F7D0W2; -.
DR STRING; 47917.AV650_24285; -.
DR GeneID; 30318830; -.
DR KEGG; sfw:WN53_01525; -.
DR PATRIC; fig|47917.8.peg.319; -.
DR Proteomes; UP000034699; Chromosome.
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; 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; PF13380; CoA_binding_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:UP000034699};
KW Transferase {ECO:0000313|EMBL:AKG67930.1}.
FT DOMAIN 487..523
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 726..878
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 883 AA; 96746 MW; DDF7FBCB2EE3EB72 CRC64;
MSQRGLEALL RPKSIAVLGA SQQPGRAGYL MMRNLLAGGF TGPILPVTPR YKAVCGVMAY
PDVASLPLTP DLAVLCTNAQ RNLALIEALG ERGCKTAIVL SSPVEQFAEL KATAQRYSMR
LLGPNSLGLL APWQGINASF SPVPIQKGKL AFISQSAAVA NTILDWAQQR EVGFSYFIAL
GDSLDIDVDD LLDFLARDSK TSAILLYLEN INDARRFLSA SRSASRNKPI LVIKSGRSQQ
AQQLLNSQQG LDAAYDAAIQ RAGLLRVQDT HELFSAVETL SHMHPLRGER LMIISNGAAP
AAMALDQLIS RNGKLATLTD ETQEKLSAAL PEFIRPGNPI DLRDDATPKR YLAALQPLLD
SHDYDALLLI HAPSAASPGT ETAERLIEAI RQHPRGKRIT LLTNWCGEYS SQEARRLFTE
AGIPTYRTPE GAVTAFMHMV EYRRNQKQLK ETPALPIGLT ANTAAAHQLI HQALAEGASQ
LDTHEVQPIL QAYGLSTLPT WIASDSAEAV HIAEQIGYPV ALKLRSPDIS HKSEVQGVML
YLRTATEVQR AAEAILDRVK RTYPQARIHG LLVQSMANRA GAQELRIAVE QDATFGPLIM
LGEGGIEWRK ENQVAVALPP LNMALARYLV LQAVKGGKIR GRSALRPLDI PGLSRLLVQV
SNLILDCPEI SRLDIHPVLA SGSEFTLLDV SMQLTPFSGD PQARLAIRPY PHELEETIEL
KDGSQCLFRP ILPEDEPALK HFIDRVTKED LYYRYFSEIN EFSHDDLANM TQIDYDREMA
FVAVRDGEEI IGVTRALSDP DNTDAEFAVL VRSDLKGLGL GRQLLMKMIG YARAQGLTRL
TGITMPNNRG MVTLAQKLGF KVDVQIDEGI VNLTLPLQDG ATP
//