ID A0A158PN67_ANISI Unreviewed; 585 AA.
AC A0A158PN67;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase {ECO:0000256|ARBA:ARBA00041297};
GN ORFNames=ASIM_LOCUS10716 {ECO:0000313|EMBL:VDK43506.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001115801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001115801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK43506.1, ECO:0000313|Proteomes:UP000267096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; UYRR01031014; VDK43506.1; -; Genomic_DNA.
DR WBParaSite; ASIM_0001115801-mRNA-1; ASIM_0001115801-mRNA-1; ASIM_0001115801.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; 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; 2.
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:UP000267096}.
FT DOMAIN 13..77
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 115..363
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
FT DOMAIN 468..553
FT /note="AMP-binding enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13193"
SQ SEQUENCE 585 AA; 67064 MW; A797277085A9EAFF CRC64;
MIANRPMHEI FLENVRKCPN KEAYVEIGTH RRVTFMQFND LTNRYANFFK DEGYEFGDVI
SLFMSNSIDY VAVWMGLTLE TVFGNGLMNQ CKIYVIDTTA ENHLNVFHIK DKILKQKADE
PKSPSSLNFQ SILCYIYTSG TTGHPKPAII KHFSTFCHYV NEMSVIMQAC NEPKLRFYVM
VMGCGKSFNI MSTDRIYVTM PMYHSSAGII GVGQALLNAS TCVIRKKFSA SNFWIDCINY
ECTVSQYIGE MCRYLLAQKE IPEEKLHKVR LMYGNGLRIE IWRDFVTRFH IAKIGEFYGS
TEGNSNIVNI DNRIGACGFF PVYAFLAPVY PVRLLKTDEK TGEILRNKNG LCIACRPGET
GEMVGLIKNN DLLLRFEGYV NNEETNKKII RNAFRFGDAV FSSGDLIYWD EYGYLYFKDR
RGDTFRYGTR LGQLPLGRFL ESIENQSERK IPRHHADKWK GENVSTTEVE GILQPIKELS
NIIVYGVEIP TVIFCVTEQE GRAGMVAVVS KEGTSHDQLI DKISSRLKAN LPQYAIPVFL
RFCDKLDMTG TFKLKKVNLQ RDGFNLERCC DDAIYLWNSS NAKYM
//