ID   Q6AIE6_DESPS            Unreviewed;       591 AA.
AC   Q6AIE6;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE            EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN   OrderedLocusNames=DPPB37 {ECO:0000313|EMBL:CAG37901.1};
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OG   Plasmid large {ECO:0000313|Proteomes:UP000000602}.
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG37901.1, ECO:0000313|Proteomes:UP000000602};
RN   [1] {ECO:0000313|EMBL:CAG37901.1, ECO:0000313|Proteomes:UP000000602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602};
RC   PLASMID=large {ECO:0000313|Proteomes:UP000000602};
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
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DR   EMBL; CR522871; CAG37901.1; -; Genomic_DNA.
DR   RefSeq; WP_011190396.1; NC_006139.1.
DR   AlphaFoldDB; Q6AIE6; -.
DR   STRING; 177439.DPPB37; -.
DR   KEGG; dps:DPPB37; -.
DR   eggNOG; COG0365; Bacteria.
DR   HOGENOM; CLU_000022_3_6_7; -.
DR   OrthoDB; 9801302at2; -.
DR   Proteomes; UP000000602; Plasmid large.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR   PANTHER; PTHR24095:SF14; ACETYL-COENZYME A SYNTHETASE 1; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000602}.
FT   DOMAIN          61..438
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          488..566
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   591 AA;  65732 MW;  6D585147D66EF37C CRC64;
     MKDDSGPCKA ITKAANSWAV QPNLLDYGKT CDQFSWATAR RELDGLPENK GLNIAHEAVD
     RHANGPRGDR LAIRWLGKDG GVRDFSYSDL KRQSNRFANV LRKLDIGRGE RVFTLAGRVP
     ELYFSAFGTW KNGSVFCPLF SAFGSEPIYQ RLSKGDAKVL VTTERLYKQK VAALRERLPQ
     LKHILLIDAA QDIGEGLWSL PRRMEEAADA FIIPPTDPED MAIVHFTSGT TGMPKGAVHV
     HNAVLTHYLT GKYVLDFHPG DVFWCTADPG WVSGTSYGII APLVHGVTNI IDEAEFDAKR
     WYQLLEEQQV NIWYTAPTAI RRLMRLAIDP TKQYDLSHLR CIHSVGEPLN PEAVSWGQQS
     LGLPIHDNWW QTETGGIMIA NYPAVDIRPG SMGLPLPGIE AAIVRRGTGE RVEAVTEPGT
     QGELALRPGW PSMFRAYLHE EQRYRKCFVG GWYITGDLAY RDADGYFWFV GRADDIINTS
     GHMVGPFEVE SALMEHPAVT EAGVIGKPEA LIGELVKAFV TLKPGTKPSE ELRLELIGFA
     RKKLGSAVAP KEIEFRNNLP KTRSGKIMRR LLKARELGLA EGDTSTLEVD E
//