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Database: UniProt
Entry: A0A0N0E4Z1_9PSED
LinkDB: A0A0N0E4Z1_9PSED
Original site: A0A0N0E4Z1_9PSED 
ID   A0A0N0E4Z1_9PSED        Unreviewed;       568 AA.
AC   A0A0N0E4Z1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|ARBA:ARBA00039545};
DE            EC=6.2.1.3 {ECO:0000256|ARBA:ARBA00026121};
DE   AltName: Full=Long-chain acyl-CoA synthetase {ECO:0000256|ARBA:ARBA00042773};
GN   ORFNames=PF66_01436 {ECO:0000313|EMBL:KPA91854.1};
OS   Pseudomonas fuscovaginae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=50340 {ECO:0000313|EMBL:KPA91854.1, ECO:0000313|Proteomes:UP000037931};
RN   [1] {ECO:0000313|EMBL:KPA91854.1, ECO:0000313|Proteomes:UP000037931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRRI 6609 {ECO:0000313|EMBL:KPA91854.1,
RC   ECO:0000313|Proteomes:UP000037931};
RX   PubMed=26422147;
RA   Quibod I.L., Grande G., Oreiro E.G., Borja F.N., Dossa G.S., Mauleon R.,
RA   Cruz C.V., Oliva R.;
RT   "Rice-Infecting Pseudomonas Genomes Are Highly Accessorized and Harbor
RT   Multiple Putative Virulence Mechanisms to Cause Sheath Brown Rot.";
RL   PLoS ONE 10:E0139256-E0139256(2015).
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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:KPA91854.1}.
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DR   EMBL; JSYZ01000004; KPA91854.1; -; Genomic_DNA.
DR   RefSeq; WP_054056788.1; NZ_JTBY01000023.1.
DR   AlphaFoldDB; A0A0N0E4Z1; -.
DR   STRING; 50340.PF66_01436; -.
DR   PATRIC; fig|50340.43.peg.4589; -.
DR   OrthoDB; 9803968at2; -.
DR   Proteomes; UP000037931; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR   CDD; cd05936; FC-FACS_FadD_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:SF8; LONG-CHAIN-FATTY-ACID--COA LIGASE; 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:KPA91854.1}.
FT   DOMAIN          41..434
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          485..560
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   568 AA;  63255 MW;  AD718BD7CCA0C2DE CRC64;
     MSVASLQSTE RVWVKAYHPG VPADVEAEID RYPSLREVFL EHVEKYRQRV AYVSIGTEMG
     YDEWERRVFA FTAWLQSRGV KKGDRVALMM PNCLQYPICL FGTLLAGAVV VNVNPLYTAR
     ELKHLLKDSG AETLVIFENF AHTLEQAMDG SSLKNIVVAA IGDLVGTFKG AALNFVLRHV
     QKQVPRFDLP GSIRFPAMLK QARGLKARPV ALAHDDIAFL QYTGGTTGDA KGAMLTHRNI
     LANLMQAKAW VGDQLDENRQ ETNVTLLPLY HVLSLTVNCL MFMCLGGRNI LIANPRDVKR
     VQMILRKEKF NGIVGVNTLF NGLLENDEFR ARDFSDLKLA IAGGMATHTA VARRWQEVTG
     VPIIEGYGLT ECSPVVSISP IDIKRMREGE FSGTIGVPLP STWVRFVRED GTLAEIGEEG
     ELQVRGPQVM KGYWKRPDET AKVLDADGWL STGDIGVMNA QGFIRLVDRK KDMILVSGFN
     VYPNEIEDVV ALHPGVAEVA AIGVPDQVTG ERVKIFVVRR DPGLTETQLL AHCREYLTGY
     KVPRIVEFRV EELPKTTVGK VLRRALRE
//
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