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Database: UniProt
Entry: A0A166E5P2_9EURY
LinkDB: A0A166E5P2_9EURY
Original site: A0A166E5P2_9EURY 
ID   A0A166E5P2_9EURY        Unreviewed;       556 AA.
AC   A0A166E5P2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Acetyl-coenzyme A synthetase {ECO:0000313|EMBL:KZX16306.1};
DE            EC=6.2.1.1 {ECO:0000313|EMBL:KZX16306.1};
GN   Name=acsA_1 {ECO:0000313|EMBL:KZX16306.1};
GN   ORFNames=MBCUT_09190 {ECO:0000313|EMBL:KZX16306.1};
OS   Methanobrevibacter cuticularis.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=47311 {ECO:0000313|EMBL:KZX16306.1, ECO:0000313|Proteomes:UP000077275};
RN   [1] {ECO:0000313|EMBL:KZX16306.1, ECO:0000313|Proteomes:UP000077275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11139 {ECO:0000313|EMBL:KZX16306.1,
RC   ECO:0000313|Proteomes:UP000077275};
RA   Poehlein A., Seedorf H., Daniel R.;
RT   "Genome sequence of Methanobrevibacter cuticularis DSM 11139.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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:KZX16306.1}.
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DR   EMBL; LWMW01000095; KZX16306.1; -; Genomic_DNA.
DR   RefSeq; WP_067259446.1; NZ_LWMW01000095.1.
DR   AlphaFoldDB; A0A166E5P2; -.
DR   STRING; 47311.MBCUT_09190; -.
DR   PATRIC; fig|47311.3.peg.1013; -.
DR   OrthoDB; 193284at2157; -.
DR   Proteomes; UP000077275; Unassembled WGS sequence.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
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; IPR020845; AMP-binding_CS.
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.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KZX16306.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077275}.
FT   DOMAIN          40..414
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          464..542
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
FT   COILED          137..164
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   556 AA;  63891 MW;  959EDF66D2164555 CRC64;
     MSSLLKEFVN RTDFDSYEDF KNNFDFKVPK NFNFAYDVVD RYAKEDPEKI ALIWCNDFNE
     EKIFTFKDMK KYSDKAANFF KTQGIEKGDA VMLTLKNRFE FWFCIIGLHK IGAIPVPATH
     MLKTKDIVYR IDKASIKMIV SIDNEELISE YEKAEKELNI KLKKISVGEK SLENWKNFSE
     NIKNCSGDFQ RPTGPQSTEN KDISILYFSS GTTGQPKMVK HDFRYPLAHI ITSKYWHDAI
     EDGIHHTSAD TGWMKAVWGG LYGQWIVGTS VFIYDYDRFD AVNLVEKIEK YKINTFCAPP
     TIYRFLIKED LSKYDFSNLK YITTAGEPLN PEVYNKVQEI FGLKLKEGFG QTETVISVAN
     FVWMEPKPGS MGKPAPRFNV ELLDTEGNIA DIGDEGEICI ETSSMPPGLF QGYYRNQKKT
     DEVWYDGYYH SGDTAWKDED GFLWFVGRND DIIKSSGYRI GPFEVESALI SHPSVLECAI
     TGAPDQVRGQ IVKATIVLTK GYKPSDGLKK ELQDHVKKVT APYKYPRLIE FVDELPKTIS
     GKIRRIQIRN EDKNKS
//
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