ID F5NYI5_SHIFL Unreviewed; 886 AA.
AC F5NYI5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Acetyltransferase family protein {ECO:0000313|EMBL:EGK35288.1};
GN ORFNames=SFK227_3218 {ECO:0000313|EMBL:EGK35288.1};
OS Shigella flexneri K-227.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=766147 {ECO:0000313|EMBL:EGK35288.1, ECO:0000313|Proteomes:UP000004520};
RN [1] {ECO:0000313|EMBL:EGK35288.1, ECO:0000313|Proteomes:UP000004520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K-227 {ECO:0000313|EMBL:EGK35288.1,
RC ECO:0000313|Proteomes:UP000004520};
RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., Jones K.,
RA Santana-Cruz I., Liu X.;
RL Submitted (APR-2011) 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:EGK35288.1}.
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DR EMBL; AFGY01000044; EGK35288.1; -; Genomic_DNA.
DR AlphaFoldDB; F5NYI5; -.
DR PATRIC; fig|766147.3.peg.3177; -.
DR Proteomes; UP000004520; 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; 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 Transferase {ECO:0000313|EMBL:EGK35288.1}.
FT DOMAIN 487..523
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 726..881
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 886 AA; 98019 MW; 14BFB6385F00A2A2 CRC64;
MSQRGLEALL RPKSIAVIGA SMKPNRAGYL MMRNLLAGGF NGPVLPVTPA WKAMLGVLAW
PDIASLPFTP DLAVLCTNAS RNLALLEELG EKGCKTCIIL SAPASQHEDL RACALRHNMR
LLGPNSLGLL APWQGLNASF SPVPIKRGKL AFISQSAAVS NTILDWAQQR EMGFSYFIAL
GDSLDIDVDE LLDYLARDSK TSAILLYLEQ LSDARRFVSA ARSASRNKPI LVIKSGRSPA
AQRLLNTTAG MDPAWDAAIQ RAGLLRVQDT HELFSAVETL SHMRPLRGDR LMIISNGAAP
AALALDALWS RNGKLATLSE ETCQKLRDAL PEHVAVSNPL DLRDDASSEH YVKTLDILLH
SQDFDALMVI HSPSAAAPAT ESAQVLIEAV KHHPRSKYVS LLTNWCGEHS SQEARRLFSE
AGLPTYRTPE GTITAFMHMV EYRRNQKQLR ETPALPSNLT SNTAEAHLLL QQAIAEGATS
LDTHEVQPIL QAYGMNTLPT WIASDSTEAV HIAEQIGYPV ALKLRSPDIP HKSEVQGVML
YLRTANEVQQ AANAIFDRVK MAWPQARVHG LLVQSMANRA GAQELRVVVE HDPVFGPLIM
LGEGGVEWRP EDQAVVALPP LNMNLARYLV IQGIKSKKIR ARSALRPLDV AGLSQLLVQV
SNLIVDCPEI QRLDIHPLLA SGSEFTALDV TLDISPFEGD NESRLAVRPY PHQLEEWVEL
KNGERCLFRP ILPEDEPQLQ QFISRVTKED LYYRYFSEIN EFTHEDLANM TQIDYDREMA
FVAVRRIDQT EEILGVTRAI SDPDNIDAEF AVLVRSDLKG LGLGRRLMEK LITYTRNHGL
QRLNGITMPN NRGMVALARK LGFNVDIQLE EGIVGLTLNL ARREES
//