ID A0A0S9N3G9_9BURK Unreviewed; 518 AA.
AC A0A0S9N3G9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Fatty-acid--CoA ligase {ECO:0000313|EMBL:KQP39833.1};
GN ORFNames=ASF44_08935 {ECO:0000313|EMBL:KQP39833.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP39833.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP39833.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP39833.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP39833.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP39833.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQP39833.1}.
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DR EMBL; LMNA01000023; KQP39833.1; -; Genomic_DNA.
DR RefSeq; WP_056900630.1; NZ_LMNA01000023.1.
DR AlphaFoldDB; A0A0S9N3G9; -.
DR STRING; 1736318.ASF44_08935; -.
DR OrthoDB; 9766486at2; -.
DR Proteomes; UP000051759; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR CDD; cd17631; FACL_FadD13-like; 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 PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR PANTHER; PTHR43767:SF1; NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED; 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 Ligase {ECO:0000313|EMBL:KQP39833.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051759}.
FT DOMAIN 9..374
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 424..499
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 518 AA; 56759 MW; B0AAC2BB58EF9FED CRC64;
MQLTQALHKA LREKPQAPAV VFGQRRSTYA RFCDRVARMA GALRQLGMGP GDRVAMLAMN
SDHYVEYLFG TWWGGGAINP VNVRWSAQEI AYSLDDCDTR ILLVDKFFAQ QVASLRDLSK
SVRTLIYVGD GPVPEGMLGF ETLLDAAEPV QDLRRQGDDL AAVMYTGGTT GRPKGVMLSH
ANLYLNALSS VAAVPRAWPV LGLVTAPFFH VAGCGLSLQL IQRMATQVIV PYYEEVAVLD
AIAREQVNET FLVPTMVKRL IEHPRFTEFD LKSLRMVLYG AAPIDATLLG QAMDALPGVQ
FCQAYGMTEL APTVAVLQPE DHLPGPHQAK RLRSAGKSVP IAEISIRDPE NNELPPGQVG
EICARGPMVM QGYWNKPAET EAALRGGWMH TGDGGMMDEE GYLYVVDRIK DMIVSGGENV
YSAEVENALA QLDGVSMSAV IGVPDDQWGE RVHAVVVLRP GADVDEAAVI AHCKTLIAGY
KCPRSVEFRE QLPVSPAGKL QKFVLREPYW KDRARKVN
//
