ID B2FMM9_STRMK Unreviewed; 908 AA.
AC B2FMM9;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Acyl-CoA synthetase {ECO:0000313|EMBL:CAQ47905.1};
GN OrderedLocusNames=Smlt4550 {ECO:0000313|EMBL:CAQ47905.1};
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ47905.1, ECO:0000313|Proteomes:UP000008840};
RN [1] {ECO:0000313|EMBL:CAQ47905.1, ECO:0000313|Proteomes:UP000008840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a {ECO:0000313|EMBL:CAQ47905.1,
RC ECO:0000313|Proteomes:UP000008840};
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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DR EMBL; AM743169; CAQ47905.1; -; Genomic_DNA.
DR RefSeq; WP_012481591.1; NC_010943.1.
DR AlphaFoldDB; B2FMM9; -.
DR EnsemblBacteria; CAQ47905; CAQ47905; Smlt4550.
DR KEGG; sml:Smlt4550; -.
DR PATRIC; fig|522373.3.peg.4283; -.
DR eggNOG; COG1042; Bacteria.
DR eggNOG; COG1670; Bacteria.
DR HOGENOM; CLU_007415_0_2_6; -.
DR Proteomes; UP000008840; 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:InterPro.
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; 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; PF13302; Acetyltransf_3; 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; PS51186; GNAT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008840}.
FT DOMAIN 743..895
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 908 AA; 97870 MW; 8403300D4A36F179 CRC64;
MSTYHLQSVF RPQSVAVIGG SPRQRSAGRA VMRNLRGTGF PGKVAWINPR HAEIDGIRTV
KRLKDLDWVP DLVVITAPAS IVPQVVRTAA ERGVQAAIIL TAHLGEGPGS LSAQVEAVAR
KHGLRILGPH CLGVIAPHAR LNASIAAHFP QAGDLALISE SSAIAAALVE WGVARSVGFS
AVVSLGDTMD VDFGDLLDYF ATDYRTRAIL LYVEQIKDAR KFMSAARAAA RAKPVVVVKS
GRAERVQPGS RDTHVQALAR ADDVYGAAFN RAGLLRVGAL DELFTAAESL GRLGTFPGRR
LAILSNGGGV GRLAVDQLIA LRGTLANLSD STVEKLDAVL PQGWSRSNPV DIVVDADGDR
YAAAIEALLA DNENDAVMVV NVPTAFTSSA DAAQALTRTL GLRPRHHRDK PVFAVWLGND
DQATATLNAA RVPTYPTEAE AVRGFQHLVR YREAQNALME TPPSLPQDFS VDAAAARALV
DAALANGQQW LDPLATHELL KAYGIPSAPV MHARDAHEAM DLAQPLLERG ASVALKILSP
DIPHKSEVDG VRLNLSTLPA VQSAANAILS RARQLRPDAR IDGLLVQPTI VRPKARELIV
GIADDATFGP VIVVGRGGTA VEVINDKALA LPPLDLRLAH ELIGQTRASR ILKAYGDVPA
ADERALALAL VKLAQLAADI PEVRTLDINP LLVDGKGILA LDARVAVAPS RILHKGRGHP
RFSVFPYPKE WERTIELSDG GRAFVRPVRP EDDALFRAFF ARVSDEDLRL RFFQSVKHFS
HEFIARLTQL DYARSIALVA IEPRSGEMLG AVRLHADADY HRGEYGILIR SDLKGHGIGW
RLMAIMIEYA KWLGLDVVEG QVLRQNSTML AMCQSLGFKT KLDPDDPTVM MVTLPVQQVE
VPEIPPAA
//
