ID W0U903_9FIRM Unreviewed; 555 AA.
AC W0U903;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Acetyl-CoA synthetase {ECO:0008006|Google:ProtNLM};
GN ORFNames=RBI_II00236 {ECO:0000313|EMBL:CCO06010.1};
OS Ruminococcus bicirculans (ex Wegman et al. 2014).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1160721 {ECO:0000313|EMBL:CCO06010.1, ECO:0000313|Proteomes:UP000027600};
RN [1] {ECO:0000313|EMBL:CCO06010.1, ECO:0000313|Proteomes:UP000027600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=80/3 {ECO:0000313|EMBL:CCO06010.1};
RX PubMed=23919528; DOI=10.1111/1462-2920.12217;
RA Wegmann U., Louis P., Goesmann A., Henrissat B., Duncan S.H., Flint H.J.;
RT "Complete genome of a new Firmicutes species belonging to the dominant
RT human colonic microbiota ('Ruminococcus bicirculans') reveals two
RT chromosomes and a selective capacity to utilize plant glucans.";
RL Environ. Microbiol. 16:2879-2890(2014).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; HF545617; CCO06010.1; -; Genomic_DNA.
DR AlphaFoldDB; W0U903; -.
DR STRING; 1160721.RBI_II00236; -.
DR KEGG; rus:RBI_II00236; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_59_10_9; -.
DR OrthoDB; 9778383at2; -.
DR Proteomes; UP000027600; Chromosome II.
DR GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43605:SF10; ACYL-COA SYNTHETASE MEDIUM CHAIN FAMILY MEMBER 3; 1.
DR PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598}.
FT DOMAIN 43..412
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 462..540
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 555 AA; 63200 MW; 4C62C1442D40B935 CRC64;
MSFVMADFYK RFVDEELDSE GRLKSFKLDL PENFNFSYDV IDELAKNVPD KVAMQWVNEE
GEEHIFTYKD LSEKSSQVAN MMLAHGVKKG DFVMAVLKRH YEFWFLAYGL MKIGAILVPA
TCQLKKKDYV YRFDAASISY IVATAEDDVP NQVDSALEQY SGMKEKFITH GAKEGWIDFL
SEMDKYPKTF ERIETHVTES MLMYFSSGTT GYPKMVLHKY SLAAAHIITA KHWHHLDENS
LHLTVSETGW AKCAWGKMFG QFICGATTFV YDFDRFIPAN VLKVIQDYKL TSFCAPPTMY
RFFIKEGLEN YDLSSLKYSC IAGEALNPEV FNKWYEYTGL KLMEGFGQTE GAVLVGNLYG
MEPKPGSMGK PTPLYNIGIV DNEGKPVKVG ETGEIVVYAK RGENPALFKE YYRNPEATDN
AWRFGMYHTG DTAYMDDDGY YWYVGRTDDL IKASGYRIGP FEIESILMEH PSVLECAITA
ADDAIRGKVV KATIVLAKGY TASPELAKEL QNYVKQSTAP YKYPRIVEFV DELPKTISGK
IRRVEIREND SKKNS
//
