ID E2X5C8_SHIDY Unreviewed; 886 AA.
AC E2X5C8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Acetyl-CoA synthetase {ECO:0000313|EMBL:AHA66631.1};
DE EC=6.2.1.13 {ECO:0000313|EMBL:AHA66631.1};
GN ORFNames=Asd1617_03804 {ECO:0000313|EMBL:AHA66631.1};
OS Shigella dysenteriae 1617.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=754093 {ECO:0000313|EMBL:AHA66631.1, ECO:0000313|Proteomes:UP000031647};
RN [1] {ECO:0000313|EMBL:AHA66631.1, ECO:0000313|Proteomes:UP000031647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1617 {ECO:0000313|EMBL:AHA66631.1,
RC ECO:0000313|Proteomes:UP000031647};
RA Aksomboon Vongsawan A., Kapatral V., Vaisvil B., Serichantalergs O.,
RA Hale T.L., Mason C.J.;
RT "Comparative genomics of Sd1617 to representative strains in evaluating its
RT pathogenesis.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP006736; AHA66631.1; -; Genomic_DNA.
DR RefSeq; WP_000082955.1; NZ_ADUT01000017.1.
DR AlphaFoldDB; E2X5C8; -.
DR KEGG; sdz:Asd1617_03804; -.
DR PATRIC; fig|754093.4.peg.3700; -.
DR HOGENOM; CLU_007415_0_2_6; -.
DR Proteomes; UP000031647; Chromosome.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
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 Ligase {ECO:0000313|EMBL:AHA66631.1}.
SQ SEQUENCE 886 AA; 97859 MW; 6333913F1E044FE0 CRC64;
MSQRGLEALL RPKSIAVIGA SMKPNRAGYL MMRNLLAGGF NGPVLPVTPA WKAVLGVLAW
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 LGHVAISNPL DLRDDASSEH YVKTLDILLH
SQDFDALMVI HSPSAAAPAT ESAQALIEAV KHHPRSKYVS LLTNWCGEHS SQEARRLFSE
AGLPTYRTPE GTITAFMHMV EYRRNQKQLR ETPALPSNLT SNTAKAHLLL QQAIAEGATS
LDTHEVQPIL QAYGMNTLPT WIASDSTEAV HIAEQIGYPV ALKLRSPDIP HKSEVQGVML
YLRTANEVQQ AANAIFDRVK MTWPQARVHG LLVQSMANRA GAQELRVVVE HDPVFGPLIM
LGEGGVEWRP EDQAVVALPP LNMNLARYLV IQGIKSKKIR ARSALRPLDV AGLSQLLVQV
SNLIVDCPEI QRLDIHPLLA SGSEFTALDV TLDIAPFEGD NESRLAVRPY PHQLEEWVEL
KNGERCLFRP ILPEDEPQLQ QFISRVTKED LYYRYFSEIN EFTHEDLANM TQIDYDREIA
FVAVRRIDQT EEILGVTRAI SDPDNIDAEF AVLVRSDLKG LGLGRRLMEK LITYTRDHGL
QRLNGITMPN NRGMVALARK LGFNVDIQLE EGSVGLTLNL AQREES
//