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Database: UniProt
Entry: A0A1S3LIB5_SALSA
LinkDB: A0A1S3LIB5_SALSA
Original site: A0A1S3LIB5_SALSA 
ID   A0A1S3LIB5_SALSA        Unreviewed;       699 AA.
AC   A0A1S3LIB5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Propionate--CoA ligase {ECO:0000256|ARBA:ARBA00029726};
DE            EC=6.2.1.1 {ECO:0000256|ARBA:ARBA00013275};
DE            EC=6.2.1.17 {ECO:0000256|ARBA:ARBA00012985};
GN   Name=LOC106566799 {ECO:0000313|RefSeq:XP_013990682.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013990682.1};
RN   [1] {ECO:0000313|RefSeq:XP_013990682.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_013990682.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA;
CC         Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392,
CC         ChEBI:CHEBI:456215; EC=6.2.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00000787};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20374;
CC         Evidence={ECO:0000256|ARBA:ARBA00000787};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:456215; EC=6.2.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001884};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23177;
CC         Evidence={ECO:0000256|ARBA:ARBA00001884};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   RefSeq; XP_013990682.1; XM_014135207.1.
DR   AlphaFoldDB; A0A1S3LIB5; -.
DR   Ensembl; ENSSSAT00000217157; ENSSSAP00000173034; ENSSSAG00000075232.
DR   GeneID; 106566799; -.
DR   KEGG; sasa:106566799; -.
DR   OrthoDB; 144557at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa13.
DR   Bgee; ENSSSAG00000075232; Expressed in digestive tract and 16 other cell types or tissues.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050218; F:propionate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd05966; ACS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR032387; ACAS_N.
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; PTHR24095; ACETYL-COENZYME A SYNTHETASE; 1.
DR   PANTHER; PTHR24095:SF126; ACETYL-COENZYME A SYNTHETASE, CYTOPLASMIC; 1.
DR   Pfam; PF16177; ACAS_N; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT   DOMAIN          30..90
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          98..526
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          581..659
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   699 AA;  78813 MW;  EFDB3A598F6C2E8F CRC64;
     MIPDKAPKED VFHAGGDLKK EAHVPNFEKY KELYLKSIEH PDEFWGDIAK DFYWKSKHTG
     QFMDYNFDVT KGEIYIKCME GATTNICYNV LDCNVHERRL GDKVAFYWEG NEPGDEMTVT
     YRELLQQVCQ FANVLKSQGV KKGDRVSIYM PMVVELVVAM LACVRIGAVH SIVFAGFSAE
     SLCERILDSQ CSLLITADGF YRGDKLINLK VIADDALQKC RDRSFPVQRC IMLKHLSKEV
     EAIPLSSQSP PAKRPCPDLQ QEKQKDRVKK IRPVPQVPWN PEVDQCWLSL LSGVSEECEP
     EWCDSEDPLF ILYTSGSTGK PKGVLHTIGG YMLYVATTFK LVFDYHPDDV YWCTADIGWI
     TGHSYITYGP LANGATSVLF EGLPTYPDVS RMWEIVDKYQ VTKFYTAPTA IRLLMKYGCE
     PVQKYKRDSL KVLGTVGEPI NPEAWQWYYS VVGEKRCPVV DTFWQTETGG HVLTPLPAAT
     PMKPGSATFP FFGVVPAILN ESGEELEGPS EGYLVFKQPW PGVMRTVYGN HQRFETTYFE
     QFPGYYVTGD GCRRDKDGYY WITGRIDDML NVSGHLLSTA EVESALVEHE AVVEAAVVSR
     PHPVKGESLY CFVTLTDGVS FSRTLEAQLK KQVREKIGAI ATPDFIQNAP GLPKTRSGKI
     MRRVLRKIAR NERDLGDVST LADSSVIELL FQNRCCGAV
//
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