ID   A0A1M4W1A0_9BACT        Unreviewed;       896 AA.
AC   A0A1M4W1A0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Acetyltransferase {ECO:0000313|EMBL:SHE74925.1};
GN   ORFNames=SAMN05444274_102279 {ECO:0000313|EMBL:SHE74925.1};
OS   Mariniphaga anaerophila.
OC   Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC   Mariniphaga.
OX   NCBI_TaxID=1484053 {ECO:0000313|EMBL:SHE74925.1, ECO:0000313|Proteomes:UP000184164};
RN   [1] {ECO:0000313|EMBL:SHE74925.1, ECO:0000313|Proteomes:UP000184164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26910 {ECO:0000313|EMBL:SHE74925.1,
RC   ECO:0000313|Proteomes:UP000184164};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQUM01000002; SHE74925.1; -; Genomic_DNA.
DR   RefSeq; WP_072999372.1; NZ_FQUM01000002.1.
DR   AlphaFoldDB; A0A1M4W1A0; -.
DR   STRING; 1484053.SAMN05444274_102279; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000184164; Unassembled WGS sequence.
DR   GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:InterPro.
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   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   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184164};
KW   Transferase {ECO:0000313|EMBL:SHE74925.1}.
FT   DOMAIN          497..704
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          740..894
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   896 AA;  99014 MW;  38884EEA9D8144CE CRC64;
     MAIKSLDSIF KPKRIALIGV SNNPDSVGGI TLRNLVSGGY NGVVYPVNPK REAVLGIPCF
     PNVKSLPKVP DLAVIMTSAK FVPQIVRECG EAGIRGIIIM SAGFKEAGKE GKILEQQVKD
     ERAKFPDMRV IGPNCLGILV PGLNMNVSFA AGMPKKGHVA FISQSGALCT SVLDWAYESN
     IGFSNFVSIG NSMDVSFGDL IDYFGQDPET KSIVLYVESI ADAHTFMSAA RAFSRKKPII
     VYKSGRFPES AAAAASHTGA MASEDSIYDA VFRRAGLARV FDFGDIFNFT DLVGRKRMPK
     GNRLAIVTNA GGPGVMATDS LISLGGKLVK LSDKTMERLN EYLPPFWSHG NPIDVLGDAT
     PERFATATEI VLDDENVDAA LILLTPQAMT APTAIAEAIS ELASKTTKTI MTAWMGGASM
     REGMQVFNNA GISSFQAPEQ AIKAFMTLSD YSQNLSMLYE TPKEVPVSFE YDRNELRKKY
     LKDVFPKARI LNEDDSKMLV NDYGIDTTSP IPAANEDEAV RVSEDKGYPV VMKIYSPDIT
     HKSDVGGVAL NIKSEEMVRA AFRNMMKTVS EKQPDARIDG VTIQKMVDTK GAIELIVGIK
     KDKAFGTVML VGMGGTTAEL FKDNRLEFPP LNEKLARQML ESLKIYPLLK GWRGDAPKNI
     DKLIEVLIRM SYLAADYPEI AELDINPLIV TNTDVIALDA RIVVDEEIMK NPVKDYDHLI
     LKPYPESMVK TCELKDGQTI TLRPIKPEDE PMWQEMLEGC SKESIYHRFR NDFSFESHQV
     ATQFCFIDYD REVAIVAEIE EEGKKKLVGV GRLIADPDLE TMEYAILIND KWQKKELGNM
     ITAYCAEIAK QKQIKTLLAE TTQDNKPMLS VFRKLNFKIH FNEDGSVSVK KDLTEN
//