ID A0A182PQZ8_9DIPT Unreviewed; 650 AA.
AC A0A182PQZ8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|ARBA:ARBA00041297};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI009379-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI009379-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI009379-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 AlphaFoldDB; A0A182PQZ8; -.
DR STRING; 199890.A0A182PQZ8; -.
DR EnsemblMetazoa; AEPI009379-RA; AEPI009379-PA; AEPI009379.
DR VEuPathDB; VectorBase:AEPI009379; -.
DR OrthoDB; 1650656at2759; -.
DR Proteomes; UP000075885; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43107:SF21; FATTY ACID TRANSPORT PROTEIN 1, ISOFORM F-RELATED; 1.
DR PANTHER; PTHR43107; LONG-CHAIN FATTY ACID TRANSPORT PROTEIN; 1.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 61..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 127..254
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 277..410
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 528..603
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 71983 MW; EA93C6E93D5D3508 CRC64;
PSIVDVEKGQ PENELTRQQQ ERQVAGSRWR PTSALEPFGT EPSPGESTGS RSASGDRFRL
VLLYVLQFTS VGASIAAVVL IWYYMGWEFG LPALLITLAA VFIASGWWRW WHIAFHAKNN
ATIGDIFAEF VSKQPEKACL IFEGRTWTFR EVNDYSNRLA NVFHSHGYKH GDVVGLLQEN
RPEFVATWLG LSKLGVIVPL INHNLRKNAL MHSVTVANCN ALIYGEALAE AVAEIADTLP
SAVALYQVNE AAQNPVLANA KDLTTLMQYI FIAAAISVVA GFRADDTFYT PLPLYHTAGG
MMSIGQALLF GATVVTRKKF SASQYFADCQ KYNCTIAQYI GEMCRYILAT PASAVDKAHK
VRMIFGNGLR PQIWPQFVER FNIPRVAEFY GATEGNANIV NIDNTVGAIG FVSRIIPAVY
PISIIRADPA TGYSEPLRGK DGLCQLCKPN EPGLFIGKII PNNPSRAFLG YVDKGATEKK
IVRDIFRKGD AAFLSGDLLV ADERGSLFFK DRTGDTYRWK GENVSTSEVE AEVSNACGYR
DTVVYGVEVP NLEGRAGMAA ILDPERQVDL EQLARTLKDT LPSYARPQFV RLLSKVDMTG
TFKLKKLDLQ VEGFDPSGIE DSVYYLTSKG QYELLTPEIY EQIKRGEVRL
//
