COASY_PIG
ID COASY_PIG Reviewed; 562 AA.
AC Q8MIR4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Bifunctional coenzyme A synthase;
DE Short=CoA synthase;
DE AltName: Full=NBP;
DE AltName: Full=POV-2;
DE Includes:
DE RecName: Full=Phosphopantetheine adenylyltransferase;
DE EC=2.7.7.3 {ECO:0000269|PubMed:6312972};
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:6312972};
DE AltName: Full=Dephosphocoenzyme A kinase;
DE Short=DPCOAK;
GN Name=COASY {ECO:0000250|UniProtKB:Q13057};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM19997.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 46-64; 160-177; 182-210;
RP 296-315; 340-355; 482-500 AND 519-536, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC TISSUE=Liver {ECO:0000312|EMBL:AAM19997.1};
RX PubMed=11994049; DOI=10.1042/bj20020569;
RA Aghajanian S., Worrall D.M.;
RT "Identification and characterization of the gene encoding the human
RT phosphopantetheine adenylyltransferase and dephospho-CoA kinase
RT bifunctional enzyme (CoA synthase).";
RL Biochem. J. 365:13-18(2002).
RN [2] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6312972; DOI=10.1042/bj2150153;
RA Worrall D.M., Tubbs P.K.;
RT "A bifunctional enzyme complex in coenzyme A biosynthesis: purification of
RT pantetheine phosphate adenylyltransferase and dephospho-CoA kinase.";
RL Biochem. J. 215:153-157(1983).
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 ECO:0000269|PubMed:6312972}.
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; Evidence={ECO:0000269|PubMed:6312972};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19802;
CC Evidence={ECO:0000305|PubMed:6312972};
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:6312972};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18246;
CC Evidence={ECO:0000305|PubMed:6312972};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.1 uM for dephospho-CoA (in the PPAT reaction)
CC {ECO:0000269|PubMed:11994049};
CC KM=190 uM for 4'-phosphopantetheine {ECO:0000269|PubMed:11994049};
CC KM=4.1 uM for dephospho-CoA (in the DPCK reaction)
CC {ECO:0000269|PubMed:11994049};
CC KM=330 uM for ATP (in the DPCK reaction)
CC {ECO:0000269|PubMed:11994049};
CC Vmax=8.13 umol/min/mg enzyme with dephospho-CoA as substrate (in the
CC PPAT reaction) {ECO:0000269|PubMed:11994049};
CC Vmax=4.37 umol/min/mg enzyme with dephospho-CoA as substrate (in the
CC DPCK reaction) {ECO:0000269|PubMed:11994049};
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:0000269|PubMed:11994049}.
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 -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:11994049}.
CC -!- SIMILARITY: In the central section; belongs to the eukaryotic CoaD
CC family. {ECO:0000305}.
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DR EMBL; AY094603; AAM19997.1; -; mRNA.
DR RefSeq; NP_998954.1; NM_213789.1.
DR AlphaFoldDB; Q8MIR4; -.
DR STRING; 9823.ENSSSCP00000018433; -.
DR PaxDb; Q8MIR4; -.
DR PeptideAtlas; Q8MIR4; -.
DR PRIDE; Q8MIR4; -.
DR Ensembl; ENSSSCT00005023141; ENSSSCP00005013881; ENSSSCG00005014598.
DR Ensembl; ENSSSCT00015090089; ENSSSCP00015036832; ENSSSCG00015067057.
DR Ensembl; ENSSSCT00025084032; ENSSSCP00025036562; ENSSSCG00025061029.
DR Ensembl; ENSSSCT00035026271; ENSSSCP00035009997; ENSSSCG00035020192.
DR Ensembl; ENSSSCT00050088636; ENSSSCP00050038019; ENSSSCG00050065066.
DR Ensembl; ENSSSCT00055055032; ENSSSCP00055043908; ENSSSCG00055027753.
DR Ensembl; ENSSSCT00065005586; ENSSSCP00065002482; ENSSSCG00065004053.
DR GeneID; 396688; -.
DR KEGG; ssc:396688; -.
DR CTD; 80347; -.
DR eggNOG; KOG3220; Eukaryota.
DR eggNOG; KOG3351; Eukaryota.
DR HOGENOM; CLU_027827_1_0_1; -.
DR InParanoid; Q8MIR4; -.
DR OMA; VIDCDKV; -.
DR OrthoDB; 1543581at2759; -.
DR TreeFam; TF105783; -.
DR BRENDA; 2.7.1.24; 6170.
DR BRENDA; 2.7.7.3; 6170.
DR Reactome; R-SSC-196783; Coenzyme A biosynthesis.
DR SABIO-RK; Q8MIR4; -.
DR UniPathway; UPA00241; UER00355.
DR UniPathway; UPA00241; UER00356.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q8MIR4; SS.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004140; F:dephospho-CoA kinase activity; IDA:UniProtKB.
DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.620; -; 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 Pfam; PF01121; CoaE; 1.
DR Pfam; PF01467; CTP_transf_like; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00152; TIGR00152; 1.
DR PROSITE; PS51219; DPCK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Direct protein sequencing;
KW Kinase; Mitochondrion; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..562
FT /note="Bifunctional coenzyme A synthase"
FT /id="PRO_0000173041"
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:0000250|UniProtKB:Q13057, 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"
SQ SEQUENCE 562 AA; 61749 MW; 5F66F5E8D3962381 CRC64;
MAVFRSGLLV LTTPLASLVP RLAPILTSAA RLVNHTLYVH LQPGMNLGGP AQPQSSPVQA
TFEVIDFITH LYAGADLHRH LDVRILLTNI RTKSFLPPLP SSVQNLAHPP EVVLTDFQTL
DGSQYNPVKQ QLERYATSCY SCCPQLSSVL LYPDYGPGML PVQPLDVPLP STIRPASPVA
RSAKQPVRGH QRGAVGGTFD RLHNAHKVLL SVACILAQEQ LVVGVADKDL LKSKLLPELL
QPYTERVEHL SEFLVDIKPS LSFDLIPLLD PYGPAGSDPS LEFLVVSEET YRGGMAVNRF
RLENGLEELT LYQIQLLKDL NPKENEEDKV SSSSFRQQML GNLLRPPHKR PELPPGCYVI
GLTGISGSGK SSVAQRLKGL GAYVIDSDQL GHRSYAPGGP AYQPVVEAFG TDILHKDGTI
NRKVLGSRVF GNKKQLKILT DIVWPVIAKL AREEVDQAVA EGKRVCVIDA AVLLEAGWQN
MVHEVWTVVI PETEAVRRIV ERDGLSEAAA QSRLQSQMSG QQLVDQSHVV LSTLWEPHVT
QRQVEKAWAL LQKRISEAPS DP
