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Database: UniProt
Entry: S9QU87_9RHOB
LinkDB: S9QU87_9RHOB
Original site: S9QU87_9RHOB 
ID   S9QU87_9RHOB            Unreviewed;       291 AA.
AC   S9QU87;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Acyl-coenzyme A synthetase/AMP-(Fatty) acid ligase {ECO:0000313|EMBL:EPX83152.1};
GN   ORFNames=ruthe_02769 {ECO:0000313|EMBL:EPX83152.1};
OS   Rubellimicrobium thermophilum DSM 16684.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX83152.1, ECO:0000313|Proteomes:UP000015346};
RN   [1] {ECO:0000313|EMBL:EPX83152.1, ECO:0000313|Proteomes:UP000015346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX83152.1,
RC   ECO:0000313|Proteomes:UP000015346};
RX   PubMed=24501632; DOI=10.4056/sigs.4247911;
RA   Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT   "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT   type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL   Stand. Genomic Sci. 8:480-490(2013).
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:EPX83152.1}.
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DR   EMBL; AOLV01000033; EPX83152.1; -; Genomic_DNA.
DR   AlphaFoldDB; S9QU87; -.
DR   STRING; 1123069.ruthe_02769; -.
DR   PATRIC; fig|1123069.3.peg.2746; -.
DR   HOGENOM; CLU_000022_3_0_5; -.
DR   Proteomes; UP000015346; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR032387; ACAS_N.
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; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
PE   4: Predicted;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Ligase {ECO:0000313|EMBL:EPX83152.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015346}.
FT   DOMAIN          28..84
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          86..226
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   291 AA;  32215 MW;  36841328235DC09A CRC64;
     MLDREQDRAK NGQGVAERMP RIDAAAHRRA YEASLADPDA FWREQSHRID WVRRPTRIKN
     TSFAPGHISI RWFEDGTLNV AANCIDRHAA RHGERTAIIW EPDDPAEPVR RISYAELLEQ
     VCRMAGVLRQ HGVGKGDRVV IYMPMIPEAA YAMLACARIG AIHSVVFGGF SPDALANRIT
     DCDARVVITA DTGPRGGRKT PLKQNVDAAL AQITQDMKVM VVRRTGDPVP WTQGRDIDLL
     AEMEQQPPLL PLCRDGGRGS ALHPLHLGIH RQAQGGGPYL RGLSRLCLAH A
//
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