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Database: UniProt
Entry: Q2LUQ3_SYNAS
LinkDB: Q2LUQ3_SYNAS
Original site: Q2LUQ3_SYNAS 
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
//
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