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Database: UniProt
Entry: A0A1M5BHK5_9CLOT
LinkDB: A0A1M5BHK5_9CLOT
Original site: A0A1M5BHK5_9CLOT 
ID   A0A1M5BHK5_9CLOT        Unreviewed;       698 AA.
AC   A0A1M5BHK5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Acetyltransferase {ECO:0000313|EMBL:SHF41909.1};
GN   ORFNames=SAMN02745158_03656 {ECO:0000313|EMBL:SHF41909.1};
OS   Lactonifactor longoviformis DSM 17459.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Lactonifactor.
OX   NCBI_TaxID=1122155 {ECO:0000313|EMBL:SHF41909.1, ECO:0000313|Proteomes:UP000184245};
RN   [1] {ECO:0000313|EMBL:SHF41909.1, ECO:0000313|Proteomes:UP000184245}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17459 {ECO:0000313|EMBL:SHF41909.1,
RC   ECO:0000313|Proteomes:UP000184245};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQVI01000027; SHF41909.1; -; Genomic_DNA.
DR   RefSeq; WP_072854217.1; NZ_FQVI01000027.1.
DR   AlphaFoldDB; A0A1M5BHK5; -.
DR   STRING; 1122155.SAMN02745158_03656; -.
DR   OrthoDB; 9807426at2; -.
DR   Proteomes; UP000184245; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP 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; 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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000184245};
KW   Transferase {ECO:0000313|EMBL:SHF41909.1}.
FT   DOMAIN          6..101
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
SQ   SEQUENCE   698 AA;  75828 MW;  F73F1E7FA5B5AB3B CRC64;
     MDLTKLLKPK SVAVIGASEK EGFGGDVCRN ILTYVKDRSR VYFVHPKRDQ VFGVPCHKSI
     LDIEDTVDLM IICTSQKTVV PLLRDGAKKG VGGAVVFASG YGEVGTDEGR ANEKELIETG
     EELGIAIMGP NCAGFVNYID DVQAFAFISE KRDRKGSVGV VSQSGQLCLS LMECPSMRFS
     YCISAGNGKA VQMEDYMDYL VDDENTKVVS IYIEGVKNTE KFAAVLKKAA QKKKPVIILK
     TGRSTKGGAI AASHTGSLAG SDKSFDAVLK KFGAIRVDDL EELMAMSSMM ATMPSIPEKA
     TFTSMSLSGG ETGICADVGS QYNLEFPDFE PETLASLKEQ LPSYATPNNP LDMTATLSYD
     EDLFAEALRT VMRDPNIGMV LVGYTLLLEI ADPAIHYMYK GIEKVVKEGS CKPIALLPFA
     ENTRNPEYST KLFEIGVPIL PPTVYAFKLL RYLSDFIEYH AETKTLELAP GKPASKNSYA
     LSEFNSKKEL EQYGVAVPKA IIAASLEEAI AFTKGKDTPF AMKIESADIL HKSDVGGVKL
     NISGEEAVTK AYNEIMESVT AKRPDAKING ILISPMLKAG VEMIIGVNND PQFGPMIMVG
     MGGVFVELFK DVALYPAPLN HEEALEMLKS LKSFKLLTGY RGSQPCDIDA LCDTIVGISK
     YASENKDELK ELDINPIFVY PEGEGVGVAD ALIVKYEK
//
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