ID COASY_MOUSE Reviewed; 563 AA.
AC Q9DBL7; A2BFA8; Q3TVZ2; Q8K3Y4;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 27-MAR-2024, entry version 182.
DE RecName: Full=Bifunctional coenzyme A synthase {ECO:0000305};
DE Short=CoA synthase;
DE Includes:
DE RecName: Full=Phosphopantetheine adenylyltransferase;
DE EC=2.7.7.3 {ECO:0000269|PubMed:11980892};
DE AltName: Full=Dephospho-CoA pyrophosphorylase;
DE AltName: Full=Pantetheine-phosphate adenylyltransferase;
DE Short=PPAT;
DE Includes:
DE RecName: Full=Dephospho-CoA kinase;
DE Short=DPCK;
DE EC=2.7.1.24 {ECO:0000269|PubMed:11980892};
DE AltName: Full=Dephosphocoenzyme A kinase;
DE Short=DPCOAK;
GN Name=Coasy {ECO:0000312|MGI:MGI:1918993}; Synonyms=Ukr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF HIS-203.
RC TISSUE=Embryo;
RX PubMed=11980892; DOI=10.1074/jbc.c200195200;
RA Zhyvoloup A., Nemazanyy I., Babich A., Panasyuk G., Pobigailo N.,
RA Vudmaska M., Naidenov V., Kukharenko O., Palchevskii S., Savinska L.,
RA Ovcharenko G., Verdier F., Valovka T., Fenton T., Rebholz H., Wang M.L.,
RA Shepherd P., Matsuka G., Filonenko V., Gout I.T.;
RT "Molecular cloning of CoA synthase. The missing link in CoA biosynthesis.";
RL J. Biol. Chem. 277:22107-22110(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-563.
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-461, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the fourth and fifth
CC sequential steps of CoA biosynthetic pathway. The fourth reaction is
CC catalyzed by the phosphopantetheine adenylyltransferase, coded by the
CC coaD domain; the fifth reaction is catalyzed by the dephospho-CoA
CC kinase, coded by the coaE domain. May act as a point of CoA
CC biosynthesis regulation. {ECO:0000250|UniProtKB:Q13057}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA +
CC diphosphate; Xref=Rhea:RHEA:19801, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57328,
CC ChEBI:CHEBI:61723; EC=2.7.7.3;
CC Evidence={ECO:0000269|PubMed:11980892};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19802;
CC Evidence={ECO:0000305|PubMed:11980892};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+);
CC Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216;
CC EC=2.7.1.24; Evidence={ECO:0000269|PubMed:11980892};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18246;
CC Evidence={ECO:0000305|PubMed:11980892};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 4/5.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 5/5. {ECO:0000250|UniProtKB:Q13057}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13057}.
CC Mitochondrion matrix {ECO:0000250|UniProtKB:Q13057}. Note=The protein
CC is mainly present in the mitochondrial matrix, probably anchored to the
CC inner mitochondrial membrane, but this protein is also present in cell
CC lysate. {ECO:0000250|UniProtKB:Q13057}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in kidney and
CC lowest levels in colon, lung, intestine, and spleen.
CC {ECO:0000269|PubMed:11980892}.
CC -!- SIMILARITY: In the central section; belongs to the eukaryotic CoaD
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20046.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; AF521095; AAM77669.1; -; mRNA.
DR EMBL; AK004878; BAB23636.2; -; mRNA.
DR EMBL; AK159405; BAE35057.1; -; mRNA.
DR EMBL; AK159912; BAE35475.1; -; mRNA.
DR EMBL; AK166894; BAE39099.1; -; mRNA.
DR EMBL; BX255926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020046; AAH20046.1; ALT_INIT; mRNA.
DR CCDS; CCDS25446.1; -.
DR RefSeq; NP_001292911.1; NM_001305982.1.
DR RefSeq; XP_006534320.1; XM_006534257.2.
DR RefSeq; XP_017170260.1; XM_017314771.1.
DR PDB; 2F6R; X-ray; 1.70 A; A=295-563.
DR PDBsum; 2F6R; -.
DR AlphaFoldDB; Q9DBL7; -.
DR SMR; Q9DBL7; -.
DR BioGRID; 214894; 5.
DR STRING; 10090.ENSMUSP00000102929; -.
DR iPTMnet; Q9DBL7; -.
DR PhosphoSitePlus; Q9DBL7; -.
DR SwissPalm; Q9DBL7; -.
DR REPRODUCTION-2DPAGE; Q9DBL7; -.
DR EPD; Q9DBL7; -.
DR jPOST; Q9DBL7; -.
DR MaxQB; Q9DBL7; -.
DR PaxDb; 10090-ENSMUSP00000102929; -.
DR PeptideAtlas; Q9DBL7; -.
DR ProteomicsDB; 285235; -.
DR Pumba; Q9DBL7; -.
DR Antibodypedia; 16973; 347 antibodies from 30 providers.
DR DNASU; 71743; -.
DR Ensembl; ENSMUST00000001806.10; ENSMUSP00000001806.4; ENSMUSG00000001755.13.
DR Ensembl; ENSMUST00000107308.4; ENSMUSP00000102929.4; ENSMUSG00000001755.13.
DR GeneID; 71743; -.
DR KEGG; mmu:71743; -.
DR UCSC; uc007lnc.1; mouse.
DR AGR; MGI:1918993; -.
DR CTD; 80347; -.
DR MGI; MGI:1918993; Coasy.
DR VEuPathDB; HostDB:ENSMUSG00000001755; -.
DR eggNOG; KOG3220; Eukaryota.
DR eggNOG; KOG3351; Eukaryota.
DR GeneTree; ENSGT00550000075078; -.
DR HOGENOM; CLU_027827_1_0_1; -.
DR InParanoid; Q9DBL7; -.
DR OMA; TQCLQSY; -.
DR OrthoDB; 460288at2759; -.
DR PhylomeDB; Q9DBL7; -.
DR TreeFam; TF105783; -.
DR Reactome; R-MMU-196783; Coenzyme A biosynthesis.
DR UniPathway; UPA00241; UER00355.
DR UniPathway; UPA00241; UER00356.
DR BioGRID-ORCS; 71743; 25 hits in 62 CRISPR screens.
DR ChiTaRS; Coasy; mouse.
DR EvolutionaryTrace; Q9DBL7; -.
DR PRO; PR:Q9DBL7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9DBL7; Protein.
DR Bgee; ENSMUSG00000001755; Expressed in right kidney and 258 other cell types or tissues.
DR Genevisible; Q9DBL7; MM.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004140; F:dephospho-CoA kinase activity; IDA:MGI.
DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IDA:MGI.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd02022; DPCK; 1.
DR CDD; cd02164; PPAT_CoAS; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR001977; Depp_CoAkinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00152; dephospho-CoA kinase; 1.
DR PANTHER; PTHR10695:SF64; BIFUNCTIONAL COENZYME A SYNTHASE; 1.
DR PANTHER; PTHR10695; DEPHOSPHO-COA KINASE-RELATED; 1.
DR Pfam; PF01121; CoaE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51219; DPCK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Mitochondrion; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..563
FT /note="Bifunctional coenzyme A synthase"
FT /id="PRO_0000173040"
FT DOMAIN 359..562
FT /note="DPCK"
FT REGION 179..357
FT /note="Phosphopantetheine adenylyltransferase"
FT BINDING 364..371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13057"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13057"
FT MOD_RES 461
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MUTAGEN 203
FT /note="H->A: Phosphopantetheine adenylyltransferase
FT activity abolished."
FT /evidence="ECO:0000269|PubMed:11980892"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:2F6R"
FT HELIX 370..380
FT /evidence="ECO:0007829|PDB:2F6R"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:2F6R"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:2F6R"
FT HELIX 402..409
FT /evidence="ECO:0007829|PDB:2F6R"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:2F6R"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:2F6R"
FT HELIX 422..429
FT /evidence="ECO:0007829|PDB:2F6R"
FT HELIX 433..460
FT /evidence="ECO:0007829|PDB:2F6R"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:2F6R"
FT TURN 471..477
FT /evidence="ECO:0007829|PDB:2F6R"
FT HELIX 478..481
FT /evidence="ECO:0007829|PDB:2F6R"
FT STRAND 483..489
FT /evidence="ECO:0007829|PDB:2F6R"
FT HELIX 492..503
FT /evidence="ECO:0007829|PDB:2F6R"
FT HELIX 507..515
FT /evidence="ECO:0007829|PDB:2F6R"
FT HELIX 520..525
FT /evidence="ECO:0007829|PDB:2F6R"
FT STRAND 528..532
FT /evidence="ECO:0007829|PDB:2F6R"
FT HELIX 537..554
FT /evidence="ECO:0007829|PDB:2F6R"
SQ SEQUENCE 563 AA; 62023 MW; F3D6F71E8E02621A CRC64;
MAVFRSGLLV LTTPLATLAA RLPPILTSAS RLVNHTLYVH LQPGMNLGGP AQPQASPVQA
TFEVLDFITH LYTGADLHRH LDVRILLTNI QTKSTFLPVL SSVQNLAHPP EVVLTDFQTL
DGSQYNPVKQ QLERYATSCY SCSPQLASVL LYPDYGTGEL PLEPPNALLP STIRPASPVA
RSPRQPVRGY HRGAVGGTFD RLHNAHKVLL SVACVLAQEQ LVVGVADKDL LKSKLLPELL
QPYAERVEHL TEFLVDIKPS LTFELVPLLD PYGPAGSDPT LEFLVVSEET YRGGMAVNRF
RLENGKEELA LYQIQLLKDQ SHNENEEDKV SSSSFRQRIL GNLLQPPNER PELPSGLYVL
GLTGISGSGK SSVAQRLKNL GAYIIDSDHL GHRAYAPGGP AYQPVVEAFG TDILHKDGTI
NRKVLGSRVF GNKKQMKILT DIVWPVIAKL AREEMDVAVA KGKTLCVIDA AMLLEAGWQS
MVHEVWTVVI PETEAVRRIV ERDGLSEAAA QSRLQSQMSG QQLVEQSNVV LSTLWESHVT
QSQVEKAWNL LQKRLPKAYQ TRN
//
