ID Q2LUQ3_SYNAS Unreviewed; 918 AA.
AC Q2LUQ3;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 24-JAN-2024, entry version 103.
DE SubName: Full=Acetyl-CoA synthetase / acetyltransferase (GNAT) family protein {ECO:0000313|EMBL:ABC77813.1};
DE EC=6.2.1.13 {ECO:0000313|EMBL:ABC77813.1};
GN ORFNames=SYN_02878 {ECO:0000313|EMBL:ABC77813.1};
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC77813.1, ECO:0000313|Proteomes:UP000001933};
RN [1] {ECO:0000313|EMBL:ABC77813.1, ECO:0000313|Proteomes:UP000001933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB {ECO:0000313|EMBL:ABC77813.1,
RC ECO:0000313|Proteomes:UP000001933};
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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DR EMBL; CP000252; ABC77813.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2LUQ3; -.
DR STRING; 56780.SYN_02878; -.
DR KEGG; sat:SYN_02878; -.
DR eggNOG; COG0045; Bacteria.
DR eggNOG; COG0456; Bacteria.
DR eggNOG; COG1042; Bacteria.
DR HOGENOM; CLU_007415_0_2_7; -.
DR InParanoid; Q2LUQ3; -.
DR OMA; ASHTGKL; -.
DR Proteomes; UP000001933; 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; 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; PF00583; Acetyltransf_1; 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 ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:ABC77813.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000001933}.
FT DOMAIN 521..557
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 762..918
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 918 AA; 100508 MW; 97301246FC8F71F1 CRC64;
MPIRPMRSSR PWRCLMGNLN NVFNPGSVAL IGASDREGSV GRIIFTNLLQ AKDRKIFPVN
PKKKVILGRK CFENIADISE PVDLAVIATP AKEVPELVED CGRAGIGGLV IISAGFKEIG
EEGRLLEERI TASRKKYGMR ILGPNCLGFV RPNEGLNATF LKTNPPPGHI AFISQSGALG
SAILDWAVNE HVGFSMFASL GAMSDVDFGD LIDFLGEDPD TRSILLYMEG VGNAKKFMSA
ARAFAMRKPI IVIKPGRFTE SAQAARSHTG AMAGDDAIYE AAFKRAGVLR VKEIADLFDC
AEILDSRKLP KGPRLAIVTA AGGPGVMATD ALIELGGELA RLSDESMERL NSILPPFWSK
GNPIDLLGDA DASRYAQAAQ ICLNDSGVDG VLVIYVPMDT AVPDEVAQAV IDTAKGSWKP
ILTAFMGADK VRSALEKLAR NNIPNYETPE QAVRAYVNMY QDEINLELLY ETPEELPGRE
TSQGDLKDLI VGVMKEKERL KGLISKALGE GRTLLNEDES KEFLAAYGIP TTVPSLTSSV
EEAVTVAGQI GYPVVIKIVS PDISHKTDVG GVVAGINSDE QLRHAYEGML KRVRDHAPKA
LIEGVTVQKM IEDIDYELIL GSKKDKDFGS VILFGMGGVT AELIRDFSIG LPPLNRTLAK
RLMEATKAYK LIQGWRGKPP ANLGELETIL VYFSYLIVDF PEIAEIDINP LAITGGVLCA
LDARIILDKD YRQSDAPYPH LVITPYPASL VTPLKSADGA EMVLRPIRPE DEPLERELLA
TLSEESRRTR FFSSFKNVTH EWLVLFCNID YDRHIAMVAE IKENGERKII GVARLILNPD
FDSGEIAVLV HDRFQRKGVG EELMKSVIEI GKSKGLSEIY GEVLMENEKM LGLFRKLGFA
TKRLSDGIMR SSLKLRQL
//