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Database: UniProt
Entry: T1KCB2_TETUR
LinkDB: T1KCB2_TETUR
Original site: T1KCB2_TETUR 
ID   T1KCB2_TETUR            Unreviewed;       448 AA.
AC   T1KCB2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|ARBA:ARBA00041297};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur08g07010.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur08g07010.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate +
CC         tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:65052, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|ARBA:ARBA00036436};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC         Evidence={ECO:0000256|ARBA:ARBA00036436};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a very long-chain fatty acid + ATP + CoA = a very long-chain
CC         fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:54536,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58950, ChEBI:CHEBI:138261, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000256|ARBA:ARBA00036527};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537;
CC         Evidence={ECO:0000256|ARBA:ARBA00036527};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; CAEY01001958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1KCB2; -.
DR   STRING; 32264.T1KCB2; -.
DR   EnsemblMetazoa; tetur08g07010.1; tetur08g07010.1; tetur08g07010.
DR   eggNOG; KOG1179; Eukaryota.
DR   HOGENOM; CLU_000022_46_1_1; -.
DR   OMA; GRIANKM; -.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
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; PTHR43107:SF15; FATTY ACID TRANSPORT PROTEIN 3, ISOFORM A; 1.
DR   PANTHER; PTHR43107; LONG-CHAIN FATTY ACID TRANSPORT PROTEIN; 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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104}.
FT   DOMAIN          35..205
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          325..400
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   448 AA;  49945 MW;  94800F5C1991C57D CRC64;
     MLYVFGEHIG NGIKPIQLEP LIAESTSHCV LSGHRPGTKD PCFYAYTSGT TGLPKAAVIK
     HLRVFYAAVG VWVAAGVRSR DILYVPLPLY HMIGVLGATL PIFTGSTSVI RHKFSASKYW
     EDFNRNKCTV GLYIGELCRF LLAQPPKPTD GQRQVRLVIS TGLRGAIWSE FVNRFNIKRV
     VEFYGSTEGS SSLINITGKP GAIGFLTMII PDFIVKIFYP LTIIKVDVET GEPIRGSDGL
     CQSVGSGDVG MIIAKIKEND SLYGFDGYVD QEATRKKILP NVLTHGDYYF VSGDLVTIDK
     YGYIYFKDRI GDTYRWRGEN VATNEIEAMI ARFCDHSDAA VFGVEVPGEE GKVGMAAIVD
     PSISLDLVNL LKYLRQSLPN YALPHFIRLL KELQYTGTSK ISKSDLKREG FNVNAVKDPI
     YYLDTKSMSY KLLDKDTYED IVNAHFRF
//
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