ID Q124C5_POLSJ Unreviewed; 561 AA.
AC Q124C5;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
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 OrderedLocusNames=Bpro_4225 {ECO:0000313|EMBL:ABE46117.1};
OS Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE46117.1, ECO:0000313|Proteomes:UP000001983};
RN [1] {ECO:0000313|Proteomes:UP000001983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA Stothard P., Coleman N.V.;
RT "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT relevance to biotechnology.";
RL Appl. Environ. Microbiol. 74:6405-6416(2008).
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}.
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DR EMBL; CP000316; ABE46117.1; -; Genomic_DNA.
DR RefSeq; WP_011485106.1; NC_007948.1.
DR AlphaFoldDB; Q124C5; -.
DR STRING; 296591.Bpro_4225; -.
DR KEGG; pol:Bpro_4225; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_9_4; -.
DR OrthoDB; 9766486at2; -.
DR Proteomes; UP000001983; Chromosome.
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:ABE46117.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001983}.
FT DOMAIN 30..426
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 477..551
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 561 AA; 61524 MW; E23302C749CC4C10 CRC64;
MNRHWLTSYP EGVPHEIDPE QFRSLNQLLE DSFRKNASKP FSVCMDRWMS YAQLDDLSSA
LGAWLQSLGL EPGARVAIML PNIPQFAVTM AAVLRAGYTC VNVNPLYTAR ELEHQLKDSG
ATTIVILENF AGTLAEVVER TPVKNIVMAS MGDLLGFWYG AWITFAVRHL AKLVPAYKLP
LGDGRTVTTF SQAVADGAKR SLAPAQSNLD SIAFLQYTGG TTGLSKGAVL THRNIVAAIL
QAEAWFTPAL RRIGDVSTTN NIAALPLYHI FALTLCLLTM RWGAHLTLVP NPRDFGKFIE
VLKKRPFHLL PGVNTLFNAL LQHPQFKTVD FSSLCVSQAG GMAASAGTAK QWLQVTGCPM
IEGWGMSETC AIGTNNPVTN REFTGTIGLP LPSIELAIKG EDGNSLAPGE SGEICIRGPQ
VMTGYYRQPD ENEKAFTRDG FMRTGDIGIM DERGYTKIVD RKKDMIIVSG FNVFPNELEN
VISLCPGVVE CAAIGIADDK QGEAIKVFVV KNDPTLTEDD VSAYCKQHFT GYKRPKYIEF
RDDLPKSNVG KILRRELRAA A
//
