ID Q6ALE9_DESPS Unreviewed; 591 AA.
AC Q6ALE9;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=acetate--CoA ligase {ECO:0000256|ARBA:ARBA00013275};
DE EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
GN OrderedLocusNames=DP2097 {ECO:0000313|EMBL:CAG36826.1};
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG36826.1, ECO:0000313|Proteomes:UP000000602};
RN [1] {ECO:0000313|Proteomes:UP000000602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54 {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; CR522870; CAG36826.1; -; Genomic_DNA.
DR RefSeq; WP_011189338.1; NC_006138.1.
DR AlphaFoldDB; Q6ALE9; -.
DR STRING; 177439.DP2097; -.
DR KEGG; dps:DP2097; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_59_10_7; -.
DR OrthoDB; 9801302at2; -.
DR Proteomes; UP000000602; Chromosome.
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; 65775 MW; 7FD5DE7C8FCC27F2 CRC64;
MKDDSGPCKA ITKAANSWAV QPNLLDYGKT CDQFSWATAR RELDGLPENK GLNIAHEAVD
RHANGPRGDR LAIRWLGKDG GVRDFSYSDL KRQSNRFANV LRELDIGRGE RVFTLAGRVP
ELYFSAFGTW KNGSVFCPLF SAFGSEPIYQ RLSKGDAKVL VTTERLYKQK VAALRERLPQ
LKHILLIDAA QDIGEGLWSL PRRMEEAADA FIIPPTDPED MAIVHFTSGT TGMPKGAVHV
HNAVLTHYLT GKYVLDFHPG DVFWCTADPG WVTGTSYGII APLVHGVTNI IDEAEFDAKR
WYQLLEEQQV NIWYTAPTAI RRLMRLAIDP TKQYDLSHLR CIHSVGEPLN PEAVSWGQQS
LGLPIHDNWW QTETGGIMIA NYPAVDIRPG SMGLPLPGIE AAIVRRGTGE RAEAVTEPGT
QGELALRPGW PSMFRAYLHE EQRYRKCFVG DWYITGDLAY RDADGYFWFV GRADDIIKTS
GHMVGPFEVE SALLEHPAVT EAGVIGKPEA LIGELVKAFV TLKPGTEPSE ELRLELIGFA
RKKLGSAVAP KEIEFRDNLP KTRSGKIMRR LLKARELGLA EGDTSTLEVD E
//
