ID C3JQS1_RHOER Unreviewed; 992 AA.
AC C3JQS1;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000313|EMBL:EEN86242.1};
GN ORFNames=RHOER0001_0567 {ECO:0000313|EMBL:EEN86242.1};
OS Rhodococcus erythropolis SK121.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=596309 {ECO:0000313|EMBL:EEN86242.1, ECO:0000313|Proteomes:UP000005836};
RN [1] {ECO:0000313|EMBL:EEN86242.1, ECO:0000313|Proteomes:UP000005836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK121 {ECO:0000313|EMBL:EEN86242.1,
RC ECO:0000313|Proteomes:UP000005836};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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:EEN86242.1}.
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DR EMBL; ACNO01000066; EEN86242.1; -; Genomic_DNA.
DR AlphaFoldDB; C3JQS1; -.
DR ESTHER; rhoer-c3jqs1; PHA_synth_III_C.
DR Proteomes; UP000005836; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43107:SF15; FATTY ACID TRANSPORT PROTEIN 3, ISOFORM A; 1.
DR PANTHER; PTHR43107; LONG-CHAIN FATTY ACID TRANSPORT PROTEIN; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:EEN86242.1}.
FT DOMAIN 121..338
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 451..794
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 992 AA; 106481 MW; 6C95A7F1FA7FB47D CRC64;
MGLNSKSVLG PIRRVVATAQ NGLEVVRLGG LETDATTSPF EIVERAAMYR LRRYFPDSDP
ETVGAPILLI PPMMMSANVY DVTRDQGAVG ILHEMGLDPW VVDFGSPDSE EGGWDRNLAD
HIIALSDIVD HIHRHTGKDV HISGYSQGGM FAYQAAAYRR SRNIASVITF GSPVDTLAAL
PFGIPAGLAT KGADFLADHV FNRLAVTGWM ARTGFQLLDP VKTLKMRVDF LLQLHDREAL
LPREQQRRFL ATEGWVAWSG PAVAELLKQF IVHNRMMTGG FVIKDQLVSL AEITCPILAF
VGEVDDIGQP QAVRGISQAA PRAKVYESTL RAGHFGLVVG STAANHTWPT TGEFVQWTEM
GGPLPDRIAN MVYGADLEDQ TGVSISNRII HTVASVAEVG AGVTKGISDL AAGALRGTFE
LSGEAARALP RLARLNQIQP HTKISLSQLL AEQRRKAPNG ECFLFDNRVH TYEAVNARID
NVVRGLISVG VRPAAHVGVL METRPSALAA IAALSRLGAV AVMLPPGSDI TAAVKLGSVD
RIITDPENVD AAVVTGRPVL VLGGGDARGL EVDPSHDVID LEQIDPTKVN LPGWYRPDPG
VARELAFIIF AESGGVLEAK QITNYRWALS AFGTATAADL DRGDTVYCLA PLHHSSSLLA
TIGGAMAGGS RIALSRGLNP ARFVEEIHRY GVTVVSYTWS MMREILDEDL LLIDGSHPVR
LFIGSGMPHG LWKRTTEAFD PAQVLEFYAS TEGDVILANV AGSKVGSKGR PLPGSAQVRL
AAYDPLSGRL LENGNGFVRE CAEDEVGLLL GRAGFTADLS GGAMRGLFQA GDSWIPTENL
FRRDADGDYW LIDHKNTVIS TVRGPVFTQP IVDALSSVAR VDLAVAYGVG DAPHQLAVAA
VTWRPGRQFR SAELAEALSR IAFDARPDIV HVVDEIPVGS SYRPSSTALA AAGLPAPGPR
TWFLDSESQS YKRLTKAIAA QLMPTRVSTG AR
//
