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Database: UniProt
Entry: A0A1A9N4U3_9BURK
LinkDB: A0A1A9N4U3_9BURK
Original site: A0A1A9N4U3_9BURK 
ID   A0A1A9N4U3_9BURK        Unreviewed;       557 AA.
AC   A0A1A9N4U3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=A6V37_28380 {ECO:0000313|EMBL:OAJ58771.1};
OS   Paraburkholderia ginsengiterrae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1462993 {ECO:0000313|EMBL:OAJ58771.1, ECO:0000313|Proteomes:UP000078116};
RN   [1] {ECO:0000313|EMBL:OAJ58771.1, ECO:0000313|Proteomes:UP000078116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCY85 {ECO:0000313|EMBL:OAJ58771.1,
RC   ECO:0000313|Proteomes:UP000078116};
RA   Dobritsa A.P., Kutumbaka K., Samadpour M.;
RT   "Reclassification of Paraburkholderia panaciterrae (Farh et al. 2015)
RT   Dobritsa & Samadpour 2016 as a later homotypic synonym of Paraburkholderia
RT   ginsengiterrae (Farh et al. 2015) Dobritsa & Samadpour 2016.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:OAJ58771.1}.
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DR   EMBL; LXKA01000309; OAJ58771.1; -; Genomic_DNA.
DR   RefSeq; WP_064269264.1; NZ_LXKA01000309.1.
DR   AlphaFoldDB; A0A1A9N4U3; -.
DR   STRING; 1462993.A6V36_32085; -.
DR   OrthoDB; 9766486at2; -.
DR   Proteomes; UP000078116; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:OAJ58771.1}.
FT   DOMAIN          30..421
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          472..546
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   557 AA;  61051 MW;  A28F5EB93F5CEF30 CRC64;
     MDKIWLKSYP PGVPAEIDPT RYSSVADLLD EAFREHRTKP AFVCMGKEIS YGELDVLSRK
     LAAWFQAKGL ARGARIAIMM PNVLQYPVAI AAILRAGYVV VNVNPLYTPR ELEHQLKDSG
     AEAIILLENF AVTLQAIVRN TSIKHVIVAA MGDLMGVKGA LVNFVVRKMK KMVPAWSLPG
     HVKFNTAIAE GGRYSFKPVQ QGPDDVAFLQ YTGGTTGVAK GATLLHRNLI ANVLQSEIWL
     NPVRTNRADI DQFVTVVALP LYHVFALTVC GLLTIRTGGL GVLIPNPRDI PGMIKALEGY
     PITTIPAVNT LYNALLNSPD FHKLDFSKLI AANGGGMAVQ EAVAKRWYEQ TRTPIIEGYG
     LSETSPCVTC NPVTVTEYSG TIGLPLPSTE ISIRDDEGNE VPLGQPGEIC IRGPQVMAGY
     WKRPDETAKV MTADGFFKSG DVGLMNERGF VKIVDRKKDM ILVSGFNVYP NEIEDVVAKL
     PGVFEVAAVG VPDQHSGEAV KLFVVKKDQS LTDADIFAYC KEQLTGYKRP KIVEFRTELP
     KSNVGKILRR ELRDGRV
//
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