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Database: UniProt
Entry: J0U3J3_9BURK
LinkDB: J0U3J3_9BURK
Original site: J0U3J3_9BURK 
ID   J0U3J3_9BURK            Unreviewed;       574 AA.
AC   J0U3J3;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=PMI14_04668 {ECO:0000313|EMBL:EJE50692.1};
OS   Acidovorax sp. CF316.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE50692.1, ECO:0000313|Proteomes:UP000004811};
RN   [1] {ECO:0000313|EMBL:EJE50692.1, ECO:0000313|Proteomes:UP000004811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF316 {ECO:0000313|EMBL:EJE50692.1,
RC   ECO:0000313|Proteomes:UP000004811};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJE50692.1}.
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DR   EMBL; AKJX01000168; EJE50692.1; -; Genomic_DNA.
DR   AlphaFoldDB; J0U3J3; -.
DR   PATRIC; fig|1144317.3.peg.4334; -.
DR   Proteomes; UP000004811; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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:EJE50692.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004811}.
FT   DOMAIN          47..439
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          490..564
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   574 AA;  62368 MW;  99C1BFA617073DB5 CRC64;
     MPGFHCNEKF GETRIMTDRP WLAAYPQGVP ADIDTSQYPS LVALMDEAFN KYASRVAYSF
     MGKDVSYAQT DSLSAAFAAY LQGLGLVKGD RVAIMMPNVP QYPVTVAAIL RAGFVVVNVN
     PLYTPRELEH QLKDSGAKAI VIIENFATTL QQCIANTPVK HVVLAAMGDQ LGLLKGTLVN
     YVVRNVKKMV PAYDLPGAVR FNDAVAKGTR GSFKKPDIRP DDIALLQYTG GTTGVSKGAV
     LLHRNVIANV LQSEAWNAPV MAKVPSGEQP TSVCALPLYH IFAFTVNMML SMRTGGKTIL
     IPNPRDLPAV LKELSKHTFH SFPAVNTLFN GLANHPDFDT VNWKNLKVSV GGGMAVQGAV
     AKLWLEKTGC PICEGYGLSE TSPSASCNPV TAKEYTGTIG VPIPGTTMKL LDDEGHEVTT
     LGQPGEIAIK GPQVMAGYWQ RPDETAKVMT DDGYFKSGDI GIMDERGYFK IVDRKKDMVL
     VSGFNVYPNE VEEVVANCPG VLECAVVGVP DEKTGEAVKL VIVKKDPGLT EAQVKEFCKA
     NLTGYKQPRV IEFRTELPKT PVGKILRREL RDKK
//
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