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Database: UniProt
Entry: A0A1M4S9G4_9BACT
LinkDB: A0A1M4S9G4_9BACT
Original site: A0A1M4S9G4_9BACT 
ID   A0A1M4S9G4_9BACT        Unreviewed;       683 AA.
AC   A0A1M4S9G4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Acetyltransferase {ECO:0000313|EMBL:SHE28856.1};
GN   ORFNames=SAMN02745131_00025 {ECO:0000313|EMBL:SHE28856.1};
OS   Flavisolibacter ginsengisoli DSM 18119.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Flavisolibacter.
OX   NCBI_TaxID=1121884 {ECO:0000313|EMBL:SHE28856.1, ECO:0000313|Proteomes:UP000184048};
RN   [1] {ECO:0000313|EMBL:SHE28856.1, ECO:0000313|Proteomes:UP000184048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18119 {ECO:0000313|EMBL:SHE28856.1,
RC   ECO:0000313|Proteomes:UP000184048};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQUU01000001; SHE28856.1; -; Genomic_DNA.
DR   RefSeq; WP_072833218.1; NZ_FQUU01000001.1.
DR   AlphaFoldDB; A0A1M4S9G4; -.
DR   STRING; 1121884.SAMN02745131_00025; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000184048; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR003781; CoA-bd.
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; 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; 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.
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:UP000184048};
KW   Transferase {ECO:0000313|EMBL:SHE28856.1}.
FT   DOMAIN          487..536
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   683 AA;  73330 MW;  62F0A9A495F833A7 CRC64;
     MITKELLDPE SIVIVGASND TSKPGGKVLY NILKNNFAGK IFGVNPKERE VQGVPCFANC
     NLIPEVSLAI IAIPANQVEA VMRILAYEKK CKAFILFSAG FSETGAEGKC LEKRCVKIVN
     DVGGTLVGPN CIGVITGTYK GVFAGPIPAY DPKGCDCVSA SGATMVYILE MAIPRGLKFR
     DIFSVGNSAQ VGVEDVLQYW DETFDEKRSS KIKLLYMEQI TDPKRFLKHA RSLVNKGCRI
     AAIKSGNTEA GSRAVSSHTG ALAGSNSAVS ALFRKAGIIR CYSRVELVYV AAIFTIPPLK
     GDRIAVITHA GGPGVMLTDI LVKNGMKVPQ LQGDKAAMLL SKLYPGSTVS NPIDFLATGT
     AEQLGEILDA VENDFEEIDA AVVVFGTTGM WSVDDVYMLL HEKMRTSRKP IFPILPSAIQ
     AAEEVSHFQS MGHVNFTDEV SFGYVLSRVN KMKPPFPEAV LPKIQQAKAI EIIDQSPKGY
     LQPGQVFELL QSAGIATVAQ AVVTSKEEAL LSANELGFPL VLKVSGILHK SDSGGVVPGI
     TSFQLLETVF EKLIAMPGAN GVIMQQQLTG SEIYVGAKAE DKFGHQVLCG LGGIFIEVFK
     DISSGLAPVG RDEAISMIRH LRSYPLIKGI RGKEGVNEEL IVDAILKISA LLQMVPEITE
     MDINPFIGNS TSLIAVDARI CIS
//
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