ID   G4RKH3_THETK            Unreviewed;       565 AA.
AC   G4RKH3;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Acetyl-coenzyme A synthetase {ECO:0000313|EMBL:CCC82068.1};
DE            EC=6.2.1.1 {ECO:0000313|EMBL:CCC82068.1};
GN   Name=acs {ECO:0000313|EMBL:CCC82068.1};
GN   OrderedLocusNames=TTX_1437 {ECO:0000313|EMBL:CCC82068.1};
OS   Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS   / Kra 1).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Thermoproteus.
OX   NCBI_TaxID=768679 {ECO:0000313|EMBL:CCC82068.1, ECO:0000313|Proteomes:UP000002654};
RN   [1] {ECO:0000313|EMBL:CCC82068.1, ECO:0000313|Proteomes:UP000002654}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1
RC   {ECO:0000313|Proteomes:UP000002654};
RX   PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA   Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA   Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA   Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA   Hensel R.;
RT   "The complete genome sequence of Thermoproteus tenax: a physiologically
RT   versatile member of the Crenarchaeota.";
RL   PLoS ONE 6:E24222-E24222(2011).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; FN869859; CCC82068.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4RKH3; -.
DR   STRING; 768679.TTX_1437; -.
DR   PaxDb; 768679-TTX_1437; -.
DR   KEGG; ttn:TTX_1437; -.
DR   PATRIC; fig|768679.9.peg.1458; -.
DR   eggNOG; arCOG04201; Archaea.
DR   HOGENOM; CLU_000022_59_10_2; -.
DR   Proteomes; UP000002654; Chromosome.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR   CDD; cd05971; MACS_like_3; 1.
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   InterPro; IPR049515; MACS_put.
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   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CCC82068.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002654}.
FT   DOMAIN          57..417
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          468..546
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   565 AA;  62745 MW;  06D4D565BF4001C6 CRC64;
     MNGIKYPKAY SDRLEIDIRN FSFNSYEDIY RKFIWNIPKY FNIGYAITDR AIALGRGENV
     AIYYEDDEGR REVVRFSELK TRSDAFARSL LDNGVRKGDV VGVYLYPGPE VVIALSAIYK
     IGAIALSISP LIGTEGVEYR LKHSEAKAFV TDGTKKEAIS IANRLNTIRA IYVVGSEPSG
     GKELSFEDQT KAGSAEIAET ESDEPAQLFY TSGSTGPPKG VLHAHRFLLG HIPTYQLYFE
     MAPRDGDVYW TNADWGWIGA LGDVVLPSLY FGMPVVAYRR TSGFSARRAL EVMSQYGVTA
     AFITPTALRI IRREYPEPLK DFDIKLRALS TAGESPGREL VLWASEAFKA SVNEFYGCTE
     TNLVVTNNSI WAKPGSLGKP APGHIVEVVD DKGNPLPPNA EGWIAVKLPD PVAFLGYFKN
     PEATAAKIKN GWFLIGDMGL KDAEGYLWFK GRGDDVIKVS GYRIGPEEIE EVITKHPAVL
     EAAVIGKPDP VRGTIVKAFV VLKPGIEPSD ILAREIQEFV KTRLAAYAYP REVEFVDQLP
     RTETGKLKRY ELRRRELERG NVQSG
//