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Database: UniProt
Entry: A0A0F2PFW0_9FIRM
LinkDB: A0A0F2PFW0_9FIRM
Original site: A0A0F2PFW0_9FIRM 
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
//
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