ID D6CPG0_THIA3 Unreviewed; 573 AA.
AC D6CPG0;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Acetate--coa ligase {ECO:0000313|EMBL:CAZ87890.1};
DE EC=6.2.1.1 {ECO:0000313|EMBL:CAZ87890.1};
GN OrderedLocusNames=THI_1197 {ECO:0000313|EMBL:CAZ87890.1};
OS Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=426114 {ECO:0000313|EMBL:CAZ87890.1, ECO:0000313|Proteomes:UP000002372};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=3As;
RA Genoscope - CEA;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22701 / CIP 110005 / 3As
RC {ECO:0000313|Proteomes:UP000002372};
RX PubMed=20195515; DOI=10.1371/journal.pgen.1000859;
RA Arsene-Ploetze F., Koechler S., Marchal M., Coppee J.Y., Chandler M.,
RA Bonnefoy V., Brochier-Armanet C., Barakat M., Barbe V.,
RA Battaglia-Brunet F., Bruneel O., Bryan C.G., Cleiss-Arnold J.,
RA Cruveiller S., Erhardt M., Heinrich-Salmeron A., Hommais F., Joulian C.,
RA Krin E., Lieutaud A., Lievremont D., Michel C., Muller D., Ortet P.,
RA Proux C., Siguier P., Roche D., Rouy Z., Salvignol G., Slyemi D., Talla E.,
RA Weiss S., Weissenbach J., Medigue C., Bertin P.N.;
RT "Structure, function, and evolution of the Thiomonas spp. genome.";
RL PLoS Genet. 6:E1000859-E1000859(2010).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; FP475956; CAZ87890.1; -; Genomic_DNA.
DR RefSeq; WP_013105236.1; NZ_CTRL01000016.1.
DR AlphaFoldDB; D6CPG0; -.
DR KEGG; thi:THI_1197; -.
DR eggNOG; COG0365; Bacteria.
DR HOGENOM; CLU_000022_59_10_4; -.
DR OrthoDB; 9766486at2; -.
DR Proteomes; UP000002372; Chromosome.
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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CAZ87890.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002372}.
FT DOMAIN 58..403
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 466..543
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 573 AA; 63386 MW; 2042703C0FB222F1 CRC64;
MQISHPISHP GAHAGFVQAR DLLQRHRTEY ARAYADFRWP ALDRFNWALD YFDPMAQGND
AIALWIVEED GSEARYSFAD MAQRSARMAN FLRAGGVARG DRVLLMLPNC IELWDAMLAC
IKLGAVMIPA TTLLTPTDLQ DRIVRGGVRH VICLPADTAK FHDLPQTIWT QVQGRFTAGS
APIGWTALAG AQTAAADFAP EADTRATDPL LLYFTSGTTS KPKLVLHTHQ SYPVGALATM
YWIGLQPGDV HWNISSPGWA KHAWSSFFAP WNAGAAIFAF NQSRFNAAAT LQTLSRCGIT
TLCAPPTVWR MLIQEDLKRY PVKLRELVGA GEPLNPEVIE RVRAAWGITI RDGYGQTETC
ALIGNSPGQP LKPGAMGRPM PGYRIRLVDV DGNSEEEGEV CVETEPRPTG LLVEYAGDAE
KTAQVMHDGL YHTGDVAQRD ADGYYTFVGR TDDVFKSSDY RISPFELESL LIEHPAVAEA
AVVPCPDALR LTIPKAFVSC RVGFTPSAEL ARDILLFVRE RAAPYKRIRR IEFFDLPKTI
SGKIRRVELR KIEIDRAAGV RGDLEFYEDD LPG
//