ID A0A0F2PFW0_9FIRM Unreviewed; 690 AA.
AC A0A0F2PFW0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN ORFNames=VR67_05670 {ECO:0000313|EMBL:KJS13123.1};
OS Peptococcaceae bacterium BRH_c8a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629715 {ECO:0000313|EMBL:KJS13123.1, ECO:0000313|Proteomes:UP000033493};
RN [1] {ECO:0000313|EMBL:KJS13123.1, ECO:0000313|Proteomes:UP000033493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c8a {ECO:0000313|EMBL:KJS13123.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJS13123.1}.
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DR EMBL; LADP01000016; KJS13123.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2PFW0; -.
DR STRING; 1629715.VR67_05670; -.
DR PATRIC; fig|1629715.3.peg.439; -.
DR Proteomes; UP000033493; Unassembled WGS sequence.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:InterPro.
DR GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019427; P:acetyl-CoA biosynthetic process from acetate; IEA:InterPro.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR011904; Ac_CoA_lig.
DR InterPro; IPR032387; ACAS_N.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR NCBIfam; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR PANTHER; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 58..106
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 108..512
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 576..654
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 690 AA; 76937 MW; 0D11A8CCB54224C4 CRC64;
MFLPLFITRD RRFGTVSEKE NGSGAHYAVH WQDEDNINPP AEFIGQANMT DPGVFDRFSL
DKFPECFKEF ADLLDWDQYW HTTLDTSDAP CWNWFVGGKL NASYNCVDRH LAKYKNKTAI
HFVPEPEDEP VVHMTYQELY QRVNETAAVL RDFCGLKAGD RVTLHLPMTP ELPITMLACA
RLGIIHSQVF AGFSGQACGE RIWDSESRVL ITIDGYYRNG KLLDHKSIGD VAVEVALKEG
QEVDKVLVWQ RYPGKYASAS PMVEGRDYFV NDLLKQYVRV RVDPVPMPAE GILFLMYTSG
STGRPKGVQH SIGGYLAYVA WMSKVIQDIH PEDVYWCMAD IGWITGHSFI VYGPLAIAAS
SVIYEGLPTY PDAGRVWRIA EELDVNIFHT SPTLIRGLRK AGPDEPAKYN YKFKHMTTVG
EPIEPEVWKW YYKVVGKGKA AIVDTWWQTE TGGFLCSTIP ALSPMKAGSA GPGVPGIHPI
ILDNDGNEIP AGAGKAGNIC IKNPWPGLMQ TIWKDRDRYV ATYFERYCKD PNSKDWRDWP
YMAGDAAVMA ADGYVRILGR IDDVINVAGH RLGTKEIESA ALTVEEVAEA AVIAAKDEIK
GVVPDLYVSL KPGYEASQEL AAKISGAVST VVGKIARPRQ VFIVPDMPKT RSGKIMRRIL
ASISNRADVG DVTSLSNPEI VEQIRKQVQD
//