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Protein

Bifunctional coenzyme A synthase

Gene

Coasy

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation.

Catalytic activityi

ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA.1 Publication
ATP + 3'-dephospho-CoA = ADP + CoA.1 Publication

Pathwayi: coenzyme A biosynthesis

This protein is involved in step 4 and 5 of the subpathway that synthesizes CoA from (R)-pantothenate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Pantothenate kinase 3 (Pank3), Pantothenate kinase 4 (Pank4), Pantothenate kinase 1 (Pank1)
  2. Phosphopantothenate--cysteine ligase (Ppcs)
  3. Phosphopantothenoylcysteine decarboxylase (Ppcdc)
  4. Bifunctional coenzyme A synthase (Coasy)
  5. Bifunctional coenzyme A synthase (Coasy)
This subpathway is part of the pathway coenzyme A biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CoA from (R)-pantothenate, the pathway coenzyme A biosynthesis and in Cofactor biosynthesis.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi364 – 3718ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • dephospho-CoA kinase activity Source: MGI
  • pantetheine-phosphate adenylyltransferase activity Source: MGI

GO - Biological processi

  • coenzyme A biosynthetic process Source: MGI

Keywords - Molecular functioni

Kinase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Coenzyme A biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-196783. Coenzyme A biosynthesis.
UniPathwayiUPA00241; UER00355.
UPA00241; UER00356.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional coenzyme A synthase
Short name:
CoA synthase
Including the following 2 domains:
Phosphopantetheine adenylyltransferase (EC:2.7.7.3)
Alternative name(s):
Dephospho-CoA pyrophosphorylase
Pantetheine-phosphate adenylyltransferase
Short name:
PPAT
Dephospho-CoA kinase (EC:2.7.1.24)
Short name:
DPCK
Alternative name(s):
Dephosphocoenzyme A kinase
Short name:
DPCOAK
Gene namesi
Name:Coasy
Synonyms:Ukr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1918993. Coasy.

Subcellular locationi

  • Cytoplasm By similarity
  • Mitochondrion matrix By similarity

  • Note: The protein is mainly present in the mitochondrial matrix, probably anchored to the inner mitochondrial membrane, but this protein is also present in cell lysate.By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi203 – 2031H → A: Phosphopantetheine adenylyltransferase activity abolished. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 563563Bifunctional coenzyme A synthasePRO_0000173040Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei177 – 1771PhosphoserineBy similarity
Modified residuei182 – 1821PhosphoserineBy similarity
Modified residuei461 – 4611N6-succinyllysineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9DBL7.
MaxQBiQ9DBL7.
PaxDbiQ9DBL7.
PeptideAtlasiQ9DBL7.
PRIDEiQ9DBL7.

2D gel databases

REPRODUCTION-2DPAGEQ9DBL7.

PTM databases

iPTMnetiQ9DBL7.
PhosphoSiteiQ9DBL7.
SwissPalmiQ9DBL7.

Expressioni

Tissue specificityi

Widely expressed with highest levels in kidney and lowest levels in colon, lung, intestine, and spleen.1 Publication

Gene expression databases

BgeeiQ9DBL7.
CleanExiMM_COASY.
GenevisibleiQ9DBL7. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiQ9DBL7. 2 interactions.
MINTiMINT-1855415.
STRINGi10090.ENSMUSP00000001806.

Structurei

Secondary structure

1
563
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi358 – 3647Combined sources
Helixi370 – 38011Combined sources
Beta strandi383 – 3864Combined sources
Helixi387 – 3948Combined sources
Helixi402 – 4098Combined sources
Helixi411 – 4133Combined sources
Beta strandi418 – 4203Combined sources
Helixi422 – 4298Combined sources
Helixi433 – 46028Combined sources
Beta strandi465 – 4695Combined sources
Turni471 – 4777Combined sources
Helixi478 – 4814Combined sources
Beta strandi483 – 4897Combined sources
Helixi492 – 50312Combined sources
Helixi507 – 5159Combined sources
Helixi520 – 5256Combined sources
Beta strandi528 – 5325Combined sources
Helixi537 – 55418Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F6RX-ray1.70A295-563[»]
ProteinModelPortaliQ9DBL7.
SMRiQ9DBL7. Positions 194-556.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9DBL7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini359 – 562204DPCKAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni179 – 357179Phosphopantetheine adenylyltransferaseAdd
BLAST

Sequence similaritiesi

In the central section; belongs to the eukaryotic CoaD family.Curated

Phylogenomic databases

eggNOGiKOG3220. Eukaryota.
KOG3351. Eukaryota.
COG0237. LUCA.
COG1019. LUCA.
GeneTreeiENSGT00550000075078.
HOGENOMiHOG000232117.
HOVERGENiHBG051059.
InParanoidiQ9DBL7.
KOiK02318.
OMAiAWNLLQK.
OrthoDBiEOG7NKKKK.
PhylomeDBiQ9DBL7.
TreeFamiTF105783.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00376. Dephospho_CoA_kinase.
InterProiIPR004821. Cyt_trans-like.
IPR001977. Depp_CoAkinase.
IPR027417. P-loop_NTPase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01121. CoaE. 1 hit.
PF01467. CTP_transf_like. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00152. TIGR00152. 1 hit.
PROSITEiPS51219. DPCK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DBL7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVFRSGLLV LTTPLATLAA RLPPILTSAS RLVNHTLYVH LQPGMNLGGP
60 70 80 90 100
AQPQASPVQA TFEVLDFITH LYTGADLHRH LDVRILLTNI QTKSTFLPVL
110 120 130 140 150
SSVQNLAHPP EVVLTDFQTL DGSQYNPVKQ QLERYATSCY SCSPQLASVL
160 170 180 190 200
LYPDYGTGEL PLEPPNALLP STIRPASPVA RSPRQPVRGY HRGAVGGTFD
210 220 230 240 250
RLHNAHKVLL SVACVLAQEQ LVVGVADKDL LKSKLLPELL QPYAERVEHL
260 270 280 290 300
TEFLVDIKPS LTFELVPLLD PYGPAGSDPT LEFLVVSEET YRGGMAVNRF
310 320 330 340 350
RLENGKEELA LYQIQLLKDQ SHNENEEDKV SSSSFRQRIL GNLLQPPNER
360 370 380 390 400
PELPSGLYVL GLTGISGSGK SSVAQRLKNL GAYIIDSDHL GHRAYAPGGP
410 420 430 440 450
AYQPVVEAFG TDILHKDGTI NRKVLGSRVF GNKKQMKILT DIVWPVIAKL
460 470 480 490 500
AREEMDVAVA KGKTLCVIDA AMLLEAGWQS MVHEVWTVVI PETEAVRRIV
510 520 530 540 550
ERDGLSEAAA QSRLQSQMSG QQLVEQSNVV LSTLWESHVT QSQVEKAWNL
560
LQKRLPKAYQ TRN
Length:563
Mass (Da):62,023
Last modified:June 27, 2003 - v2
Checksum:iF3D6F71E8E02621A
GO

Sequence cautioni

The sequence AAH20046.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF521095 mRNA. Translation: AAM77669.1.
AK004878 mRNA. Translation: BAB23636.2.
AK159405 mRNA. Translation: BAE35057.1.
AK159912 mRNA. Translation: BAE35475.1.
AK166894 mRNA. Translation: BAE39099.1.
BX255926 Genomic DNA. Translation: CAM24464.1.
BC020046 mRNA. Translation: AAH20046.1. Different initiation.
CCDSiCCDS25446.1.
RefSeqiNP_001292911.1. NM_001305982.1.
XP_006534318.1. XM_006534255.1.
XP_006534320.1. XM_006534257.1.
UniGeneiMm.182271.
Mm.486485.

Genome annotation databases

EnsembliENSMUST00000001806; ENSMUSP00000001806; ENSMUSG00000001755.
ENSMUST00000107308; ENSMUSP00000102929; ENSMUSG00000001755.
GeneIDi71743.
KEGGimmu:71743.
UCSCiuc007lnc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF521095 mRNA. Translation: AAM77669.1.
AK004878 mRNA. Translation: BAB23636.2.
AK159405 mRNA. Translation: BAE35057.1.
AK159912 mRNA. Translation: BAE35475.1.
AK166894 mRNA. Translation: BAE39099.1.
BX255926 Genomic DNA. Translation: CAM24464.1.
BC020046 mRNA. Translation: AAH20046.1. Different initiation.
CCDSiCCDS25446.1.
RefSeqiNP_001292911.1. NM_001305982.1.
XP_006534318.1. XM_006534255.1.
XP_006534320.1. XM_006534257.1.
UniGeneiMm.182271.
Mm.486485.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F6RX-ray1.70A295-563[»]
ProteinModelPortaliQ9DBL7.
SMRiQ9DBL7. Positions 194-556.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DBL7. 2 interactions.
MINTiMINT-1855415.
STRINGi10090.ENSMUSP00000001806.

PTM databases

iPTMnetiQ9DBL7.
PhosphoSiteiQ9DBL7.
SwissPalmiQ9DBL7.

2D gel databases

REPRODUCTION-2DPAGEQ9DBL7.

Proteomic databases

EPDiQ9DBL7.
MaxQBiQ9DBL7.
PaxDbiQ9DBL7.
PeptideAtlasiQ9DBL7.
PRIDEiQ9DBL7.

Protocols and materials databases

DNASUi71743.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001806; ENSMUSP00000001806; ENSMUSG00000001755.
ENSMUST00000107308; ENSMUSP00000102929; ENSMUSG00000001755.
GeneIDi71743.
KEGGimmu:71743.
UCSCiuc007lnc.1. mouse.

Organism-specific databases

CTDi80347.
MGIiMGI:1918993. Coasy.

Phylogenomic databases

eggNOGiKOG3220. Eukaryota.
KOG3351. Eukaryota.
COG0237. LUCA.
COG1019. LUCA.
GeneTreeiENSGT00550000075078.
HOGENOMiHOG000232117.
HOVERGENiHBG051059.
InParanoidiQ9DBL7.
KOiK02318.
OMAiAWNLLQK.
OrthoDBiEOG7NKKKK.
PhylomeDBiQ9DBL7.
TreeFamiTF105783.

Enzyme and pathway databases

UniPathwayiUPA00241; UER00355.
UPA00241; UER00356.
ReactomeiR-MMU-196783. Coenzyme A biosynthesis.

Miscellaneous databases

ChiTaRSiCoasy. mouse.
EvolutionaryTraceiQ9DBL7.
PROiQ9DBL7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBL7.
CleanExiMM_COASY.
GenevisibleiQ9DBL7. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00376. Dephospho_CoA_kinase.
InterProiIPR004821. Cyt_trans-like.
IPR001977. Depp_CoAkinase.
IPR027417. P-loop_NTPase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01121. CoaE. 1 hit.
PF01467. CTP_transf_like. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00152. TIGR00152. 1 hit.
PROSITEiPS51219. DPCK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF HIS-203.
    Tissue: Embryo.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-563.
    Strain: FVB/N.
    Tissue: Mammary gland.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCOASY_MOUSE
AccessioniPrimary (citable) accession number: Q9DBL7
Secondary accession number(s): A2BFA8, Q3TVZ2, Q8K3Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 27, 2003
Last modified: July 6, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.