ID A0A090LAZ4_STRRB Unreviewed; 793 AA.
AC A0A090LAZ4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=SRAE_1000353100 {ECO:0000313|EMBL:CEF65278.1,
GN ECO:0000313|WBParaSite:SRAE_1000353100.1,
GN ECO:0000313|WormBase:SRAE_1000353100};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF65278.1};
RN [1] {ECO:0000313|EMBL:CEF65278.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_1000353100.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF65278.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_1000353100.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
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; LN609528; CEF65278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090LAZ4; -.
DR STRING; 34506.A0A090LAZ4; -.
DR EnsemblMetazoa; SRAE_1000353100.1; SRAE_1000353100.1; WBGene00260148.
DR WBParaSite; SRAE_1000353100.1; SRAE_1000353100.1; WBGene00260148.
DR WormBase; SRAE_1000353100; SRP06493; WBGene00260148; -.
DR OrthoDB; 443463at2759; -.
DR Proteomes; UP000035682; Chromosome X.
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:CEF65278.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Reference proteome {ECO:0000313|Proteomes:UP000035682}.
FT DOMAIN 169..597
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 793 AA; 90990 MW; 582831278C3E06C6 CRC64;
MLKKVVKFKC LDRKNYIHIS SQVNKSMTYN HTPTAHEKIH KYHKILLRSE EITKKDVPML
TKTCLNITKK CFALADIITH IPNIILEKEK NQIKLSRKKK SIKIEEDDFC KIFSNPKNKN
GNIVESSFQN ITTLDKYIDY SFKKFSNQKL LGERKIEKIY EYKDNYGIKT KLIEQSSYEW
ETYDDVYNNI QKIRSGLKKF GLKKGDKVLF YSDTRKEVLT TMLACIKEGI IVSTYSPNMS
LKEINTVLND LNVNTIITEE AQFDKLVKIC QYSKKINQIV YFKDKHRLSK HGSNKPVKIN
ERKLIPTKIV EKIKTILPYD EFLNYSPINK PLENVNIEKN DISFICYTSG TTSQPKGCTL
THSNLISNIV GIKNEICFNH SNPTYVAYLP LSYIFEICGE LLCLGKGVRI GYSTTTTLTK
KSMKVIPGTN GDLDVLKPTI VPSVPTMLNR FKRAVCEELM KKSELEQKLF TLCYNRKLNR
KMKGLSTPIL DKTIFKITSS FLGGKVNTII CGGAPLDKDL QRFCQIISNS TFIQGYGATE
GCAVALSSPD DITTGNVGGP TITTNFMITN WNEGGYDIKN NEGELLISGP CVINNYYKNY
NDESFVKRNG IKWFKTGDIV KIRNDGAIMV IGRKKEFIKN ANGEFISLNK IEKTLLNCIY
VKQICVIVNP KLDYTSAIVV INKDAIKKLG EKVELKENII NLCKNKLIRS TVVYTFEEEF
KEILAKYEIP RKVILVSETF NQENGMLTSS GKLRRKVIEE FYKNIIELSY TPYKDELIEP
EHLNENYIEQ KKR
//