ID E2AYR1_CAMFO Unreviewed; 707 AA.
AC E2AYR1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=long-chain-fatty-acid--CoA ligase {ECO:0000256|ARBA:ARBA00026121};
DE EC=6.2.1.3 {ECO:0000256|ARBA:ARBA00026121};
GN ORFNames=EAG_10800 {ECO:0000313|EMBL:EFN61424.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN61424.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00024484};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000256|ARBA:ARBA00024484};
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DR EMBL; GL443983; EFN61424.1; -; Genomic_DNA.
DR RefSeq; XP_011266369.1; XM_011268067.2.
DR AlphaFoldDB; E2AYR1; -.
DR STRING; 104421.E2AYR1; -.
DR EnsemblMetazoa; XM_011268067.3; XP_011266369.1; LOC105257453.
DR GeneID; 105257453; -.
DR InParanoid; E2AYR1; -.
DR OMA; CPMINGY; -.
DR OrthoDB; 443463at2759; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; PTHR43272:SF83; ACYL-COA SYNTHETASE LONG-CHAIN, ISOFORM J; 1.
DR PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EFN61424.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311}.
FT DOMAIN 117..528
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 707 AA; 79272 MW; A9C5BFAAF4BB1FBA CRC64;
MEGFWISGAI HAIKALSYVY DLLTFPVYLI LQRPWEKRKA SRRIKARPIS KDDCQVTYRS
VDPPGSMHIM LEREKVDTLE KVLLWVVKMH GDKRCLGTRQ ILAEEDEPQP NGRIFKKYKM
GEYKWKSFND VDRLAISFGR GLVELGMKPR KNVVIFAETR AEWMIAAHAC FKQNFTVVTI
YATLGDEAIA HGINETEVDT VITSHDLLPK FKRLLEMVPE VKTIIYMEDQ LKSTDTKGYK
EGVRLVPFSD VVKMGNESKA SSTSPKSSDT AIIMYTSGST GVPKGVILSH KNIISTLKAF
SDAVQIRSDD VFLGFLPLAH VFELLAESVC LLNGVPIGYS SPLTLIDSSS KIQRGSKGDA
SVLHPTCLTA VPLILDRISK GINEKVKKSG PFRQAIFNFA YEYKLKWTKR GYETPLFDKY
IFGAAKQVLG SRVRLVLSGG APLSPDTHNQ VKLCLCVTVT QGYGLTETSS CATVMDMYDR
TTGRVGAPTT VCDIRLENWE EAGYRVTDHP HPRGEIVIGG DIVSAGYYKL PDKTKEDFFQ
EDGRQWFRTG DIGEFHPDGS IKIIDRKKDL VKLQLGEYVS LGKVESELKT CPVVENICVY
GDANKAYTVA LVVPNQQYLE EIATNQGITG KSLEELCNDP QIEKAVLQEL VEQAKKCKLQ
RFEIPGAVKL CAEQWSPDMG LVTAAFKLKR KAVQERYQHE INRMYAS
//
