ID F1QAA7_DANRE Unreviewed; 698 AA. AC F1QAA7; A0A8M1P9T3; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 3. DT 27-MAR-2024, entry version 90. 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=acss2 {ECO:0000313|Ensembl:ENSDARP00000112054, GN ECO:0000313|RefSeq:NP_001315282.1, GN ECO:0000313|ZFIN:ZDB-GENE-040718-388}; GN Synonyms=fa04c03 {ECO:0000313|RefSeq:NP_001315282.1}, fj80b06 GN {ECO:0000313|RefSeq:NP_001315282.1}, fj80h04 GN {ECO:0000313|RefSeq:NP_001315282.1}, wu:fa04c03 GN {ECO:0000313|RefSeq:NP_001315282.1}, wu:fj80b06 GN {ECO:0000313|RefSeq:NP_001315282.1}, wu:fj80h04 GN {ECO:0000313|RefSeq:NP_001315282.1}, zgc:92200 GN {ECO:0000313|RefSeq:NP_001315282.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000112054}; RN [1] {ECO:0000313|RefSeq:NP_001315282.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315282.1}; RX PubMed=15520368; DOI=10.1073/pnas.0407241101; RA Song H.D., Sun X.J., Deng M., Zhang G.W., Zhou Y., Wu X.Y., Sheng Y., RA Chen Y., Ruan Z., Jiang C.L., Fan H.Y., Zon L.I., Kanki J.P., Liu T.X., RA Look A.T., Chen Z.; RT "Hematopoietic gene expression profile in zebrafish kidney marrow."; RL Proc. Natl. Acad. Sci. U.S.A. 101:16240-16245(2004). RN [2] {ECO:0000313|RefSeq:NP_001315282.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315282.1}; RX PubMed=16109975; RA Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R., RA Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.; RT "The zebrafish gene map defines ancestral vertebrate chromosomes."; RL Genome Res. 15:1307-1314(2005). RN [3] {ECO:0000313|RefSeq:NP_001315282.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315282.1}; RX PubMed=17762044; DOI=10.1194/jlr.M700378-JLR200; RA Watkins P.A., Maiguel D., Jia Z., Pevsner J.; RT "Evidence for 26 distinct acyl-coenzyme A synthetase genes in the human RT genome."; RL J. Lipid Res. 48:2736-2750(2007). RN [4] {ECO:0000313|Ensembl:ENSDARP00000112054} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000112054}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [5] {ECO:0000313|Ensembl:ENSDARP00000112054, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000112054}; RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [6] {ECO:0000313|RefSeq:NP_001315282.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001315282.1}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CT027560; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CU137717; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001315282.1; NM_001328353.1. DR PaxDb; 7955-ENSDARP00000112054; -. DR Ensembl; ENSDART00000125122; ENSDARP00000112054; ENSDARG00000037781. DR Ensembl; ENSDART00000125122.4; ENSDARP00000112054.3; ENSDARG00000037781.8. DR GeneID; 436914; -. DR KEGG; dre:436914; -. DR AGR; ZFIN:ZDB-GENE-040718-388; -. DR CTD; 55902; -. DR ZFIN; ZDB-GENE-040718-388; acss2. DR eggNOG; KOG1175; Eukaryota. DR HOGENOM; CLU_000022_3_6_1; -. DR OMA; MIGHYIT; -. DR OrthoDB; 144557at2759; -. DR PhylomeDB; F1QAA7; -. DR TreeFam; TF300417; -. DR Reactome; R-DRE-2151201; Transcriptional activation of mitochondrial biogenesis. DR Reactome; R-DRE-71384; Ethanol oxidation. DR Proteomes; UP000000437; Alternate scaffold 23. DR Proteomes; UP000000437; Chromosome 23. DR Bgee; ENSDARG00000037781; Expressed in granulocyte and 27 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0003987; F:acetate-CoA ligase activity; IBA:GO_Central. 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:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central. 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 1: Evidence at protein level; 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 Proteomics identification {ECO:0007829|PeptideAtlas:F1QAA7}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}. FT DOMAIN 30..90 FT /note="Acetyl-coenzyme A synthetase N-terminal" FT /evidence="ECO:0000259|Pfam:PF16177" FT DOMAIN 98..525 FT /note="AMP-dependent synthetase/ligase" FT /evidence="ECO:0000259|Pfam:PF00501" FT DOMAIN 580..658 FT /note="AMP-binding enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF13193" FT REGION 241..273 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 257..271 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 698 AA; 78599 MW; 7FAA30766BBF8BB2 CRC64; MIPEKAPGGD VLHAPGDLKK EAHIPSFEKY KELYIKSVES PEEFWADVAK DFFWKTKYTG KFLDYNFDVT KGEIYIKCME GATTNICYNV LDRNVHERKL GDRVAFYWEG NEPGDEKTVT YRELLQQVCK FANVLKSQGV KKGDRVSIYM PMVVELVVAM LACARIGAVH SIVFAGFSSE SLCERIMDSQ CCLLITADGF YRGDKLINLK LIADEALKKC RDKSFPVEKC IMLKHLTKED EASSGSLSPP AKRACPDLQQ EKQKERVRKV RPPPQVPWNP EVDMCWHSLI GGASEECEPV WCDSEDPLFI LYTSGSTGKP KGVLHTVSGY MLYTASTFKM VFDYHSDDVY WCTADIGWIT GHSYITYGPL ANGATSVLFE GLPTYPDVSR MWEIVDKYHV SKFYTAPTAI RLLMKYGSDP VHKYKRTSLK ILGTVGEPIN PEAWQWYYNV VGEKRCPVVD TFWQTETGGH VMTPLPAATP MKPGSATFPF FGVVPAILNE SGEELEGPSE GYLVFKQPWP GVMRTVYGNH LRFETTYFKK FPGYYVTGDG CRRDKDGYYW ITGRIDDMLN VSGHLLSTAE VESALVEHEA VAEAAVVGRP HPVKGESLYC FVTLNDGINY NQKLEAELKK QVREKIGAIA TPDYIQNAPG LPKTRSGKIM RRVLRKIACN ERDLGDVSTL ADSSVIEHLF ENRCYTAV //