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Database: UniProt
Entry: A0A3Q3FF60_9LABR
LinkDB: A0A3Q3FF60_9LABR
Original site: A0A3Q3FF60_9LABR 
ID   A0A3Q3FF60_9LABR        Unreviewed;       646 AA.
AC   A0A3Q3FF60;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
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};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000018179.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000018179.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; A0A3Q3FF60; -.
DR   Ensembl; ENSLBET00000019193.1; ENSLBEP00000018179.1; ENSLBEG00000013943.1.
DR   GeneTree; ENSGT00940000166845; -.
DR   Proteomes; UP000261660; Unplaced.
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:SF146; ACETYL-COENZYME A SYNTHETASE; 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:UP000261660}.
FT   DOMAIN          29..89
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          100..455
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          528..606
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   646 AA;  73568 MW;  23DABF34F1F8A7D3 CRC64;
     MVVPESQDKM YYPPDDLKRD AHVPDFNSYL ALYRKSLENP EAFWKEIADE FFWKKPATGP
     MVQYNFDVTK GNIYIKYMEG AKTNMCYNVL DRLVREKNLG EKIAYYWEGN SPDHHMTITY
     HQLLSQVCRC ANVLKKMGVK KGDRVSIYLP MIPELVVSML ACARIGAVHS IVFAGFSSES
     LCERIMDAQS CILVTADGVY RGEKMINLKQ IADEALEKCR EKASSSVTKC LVVQHQALRT
     RSGAACNKLQ TPWDAECDVW WDEVMRDSPE ECEPEWLDAE DPLFILYTSG STGKPKGVLH
     TVAGYLLYTS LTFKYVFDYH HDDVYWCTAD IGWITGHSYI TYGPLANGAT SVLFEGIPVH
     PHVGRFWEII EKYKVTKFYT APTAIRLLMK YGQEPLQKYD LSSLKILGTV GEPINPEAWQ
     WYHEVVGQRR CPIVDTFWQT ETGGHVLTPL PAATALKPGS AVFRRPWPGI MRTVYRNHER
     FENTYFKKFP GFYVTGDGCR RDKDGYYWIT GRIDDMLNVS GHLMSTAEVE AALTEHPAVA
     EAAVVSRPHK VKGECLYCFV TLKDSKEFTH KMVEELKRLV REKIGPIATP DFIQNAPALP
     KTRSGKIMRR ILRQIARNEK DLGDLSTLAD PKVVEVLFSQ RCEAAA
//
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