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Bifunctional coenzyme A synthase (CoA synthase) (NBP) (POV-2) [Includes: Phosphopantetheine adenylyltransferase (EC 2.7.7.3) (Dephospho-CoA pyrophosphorylase) (Pantetheine-phosphate adenylyltransferase) (PPAT); Dephospho-CoA kinase (DPCK) (EC 2.7.1.24) (Dephosphocoenzyme A kinase) (DPCOAK)]

 COASY_HUMAN             Reviewed;         564 AA.
Q13057; B2RA78; B4DLU0; Q6GS23; Q8NBM7; Q8NEW1; Q8WXD4; Q9NRM3;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUN-2003, sequence version 4.
25-OCT-2017, entry version 175.
RecName: Full=Bifunctional coenzyme A synthase;
Short=CoA synthase;
AltName: Full=NBP;
AltName: Full=POV-2;
Includes:
RecName: Full=Phosphopantetheine adenylyltransferase;
EC=2.7.7.3;
AltName: Full=Dephospho-CoA pyrophosphorylase;
AltName: Full=Pantetheine-phosphate adenylyltransferase;
Short=PPAT;
Includes:
RecName: Full=Dephospho-CoA kinase;
Short=DPCK;
EC=2.7.1.24;
AltName: Full=Dephosphocoenzyme A kinase;
Short=DPCOAK;
Name=COASY; ORFNames=PSEC0106;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND VARIANT TYR-55.
PubMed=11923312; DOI=10.1074/jbc.M201708200;
Daugherty M., Polanuyer B., Farrell M., Scholle M., Lykidis A.,
de Crecy-Lagard V., Osterman A.;
"Complete reconstitution of the human coenzyme A biosynthetic pathway
via comparative genomics.";
J. Biol. Chem. 277:21431-21439(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBUNIT.
PubMed=11994049; DOI=10.1042/BJ20020569;
Aghajanian S., Worrall D.M.;
"Identification and characterization of the gene encoding the human
phosphopantetheine adenylyltransferase and dephospho-CoA kinase
bifunctional enzyme (CoA synthase).";
Biochem. J. 365:13-18(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Teratocarcinoma;
Ota T., Nishikawa T., Suzuki Y., Kawai-Hio Y., Hayashi K., Ishii S.,
Saito K., Yamamoto J., Wakamatsu A., Nagai T., Nakamura Y.,
Nagahari K., Sugano S., Isogai T.;
"HRI human cDNA sequencing project.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
TYR-55.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TYR-55.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
TYR-55.
TISSUE=Colon, Muscle, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 165-564 (ISOFORMS 1/2).
Zhu Y.-B., Han Y.;
"Molecular cloning of a NBP gene cDNA.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 332-564 (ISOFORMS 1/2).
TISSUE=Ovary;
PubMed=8529999; DOI=10.1007/BF00197407;
Montagna M., Serova O., Sylla B.S., Feunteun J., Lenoir G.M.;
"A 100-kb physical and transcriptional map around the EDH17B2 gene:
identification of three novel genes and a pseudogene of a human
homologue of the rat PRL-1 tyrosine phosphatase.";
Hum. Genet. 96:532-538(1995).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-564 (ISOFORMS 1/2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[11]
ALTERNATIVE SPLICING.
PubMed=16460672; DOI=10.1016/j.bbrc.2006.01.051;
Nemazanyy I., Panasyuk G., Breus O., Zhyvoloup A., Filonenko V.,
Gout I.T.;
"Identification of a novel CoA synthase isoform, which is primarily
expressed in the brain.";
Biochem. Biophys. Res. Commun. 341:995-1000(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-183, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
SUBCELLULAR LOCATION, AND VARIANT NBIA6 CYS-499.
PubMed=24360804; DOI=10.1016/j.ajhg.2013.11.008;
Dusi S., Valletta L., Haack T.B., Tsuchiya Y., Venco P.,
Pasqualato S., Goffrini P., Tigano M., Demchenko N., Wieland T.,
Schwarzmayr T., Strom T.M., Invernizzi F., Garavaglia B., Gregory A.,
Sanford L., Hamada J., Bettencourt C., Houlden H., Chiapparini L.,
Zorzi G., Kurian M.A., Nardocci N., Prokisch H., Hayflick S., Gout I.,
Tiranti V.;
"Exome sequence reveals mutations in CoA synthase as a cause of
neurodegeneration with brain iron accumulation.";
Am. J. Hum. Genet. 94:11-22(2014).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: 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. {ECO:0000269|PubMed:11923312}.
-!- CATALYTIC ACTIVITY: ATP + pantetheine 4'-phosphate = diphosphate +
3'-dephospho-CoA.
-!- CATALYTIC ACTIVITY: ATP + 3'-dephospho-CoA = ADP + CoA.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7.6 mM for 4'-phoshopantetheine;
KM=145 mM for ATP (in the PPAT reaction);
KM=16.7 mM for dephospho-CoA;
KM=34.4 mM for ATP (in the DPCK reaction);
-!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
(R)-pantothenate: step 4/5.
-!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
(R)-pantothenate: step 5/5.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11994049}.
-!- INTERACTION:
Q8N137:CNTROB; NbExp=3; IntAct=EBI-10227704, EBI-947360;
Q6P2E9:EDC4; NbExp=3; IntAct=EBI-745967, EBI-1006038;
Q8N8K9:KIAA1958; NbExp=3; IntAct=EBI-10227704, EBI-10181113;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion
matrix {ECO:0000269|PubMed:24360804}. Note=The protein is mainly
present in the mitochondrial matrix, probably anchored to the
inner mitochondrial membrane, but is also present in cell lysate.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=CoASy alpha;
IsoId=Q13057-1; Sequence=Displayed;
Name=2; Synonyms=CoASy beta;
IsoId=Q13057-2; Sequence=VSP_036404;
-!- TISSUE SPECIFICITY: Expressed in all tissues examined including
brain, heart, skeletal muscle, colon, thymus, spleen, kidney,
liver, small intestine, placenta, lung and peripheral blood
leukocyte. Lowest expression in peripheral blood leukocytes and
highest in kidney and liver. Isoform 2 is expressed mainly in the
brain. {ECO:0000269|PubMed:11923312}.
-!- DISEASE: Neurodegeneration with brain iron accumulation 6 (NBIA6)
[MIM:615643]: A neurodegenerative disorder associated with iron
accumulation in the brain, primarily in the basal ganglia. It is
characterized by progressive motor and cognitive dysfunction
beginning in childhood or young adulthood. Patients show
extrapyramidal motor signs, such as spasticity, dystonia, and
parkinsonism. {ECO:0000269|PubMed:24360804}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: In the central section; belongs to the eukaryotic CoaD
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA69699.1; Type=Frameshift; Positions=535; Evidence={ECO:0000305};
Sequence=AAF87955.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH06354.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH20985.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AK075415; Type=Frameshift; Positions=315; Evidence={ECO:0000305};
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EMBL; AF453478; AAL50813.1; -; mRNA.
EMBL; AY094602; AAM19996.1; -; mRNA.
EMBL; AK075415; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK297153; BAG59652.1; -; mRNA.
EMBL; AK314076; BAG36775.1; -; mRNA.
EMBL; AC067852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471152; EAW60840.1; -; Genomic_DNA.
EMBL; BC006354; AAH06354.1; ALT_INIT; mRNA.
EMBL; BC020985; AAH20985.1; ALT_INIT; mRNA.
EMBL; BC067254; AAH67254.1; -; mRNA.
EMBL; AF208536; AAF87955.1; ALT_INIT; mRNA.
EMBL; U18919; AAA69699.1; ALT_FRAME; mRNA.
EMBL; BT007168; AAP35832.1; -; mRNA.
CCDS; CCDS11429.1; -. [Q13057-1]
CCDS; CCDS45685.1; -. [Q13057-2]
RefSeq; NP_001035994.1; NM_001042529.2. [Q13057-1]
RefSeq; NP_001035997.2; NM_001042532.3. [Q13057-2]
RefSeq; NP_079509.5; NM_025233.6. [Q13057-1]
RefSeq; XP_006722179.1; XM_006722116.3. [Q13057-2]
RefSeq; XP_011523602.1; XM_011525300.1. [Q13057-1]
RefSeq; XP_016880657.1; XM_017025168.1.
UniGene; Hs.296422; -.
UniGene; Hs.742262; -.
ProteinModelPortal; Q13057; -.
BioGrid; 123254; 28.
IntAct; Q13057; 6.
MINT; MINT-1212728; -.
STRING; 9606.ENSP00000464814; -.
iPTMnet; Q13057; -.
PhosphoSitePlus; Q13057; -.
BioMuta; COASY; -.
DMDM; 32363505; -.
EPD; Q13057; -.
MaxQB; Q13057; -.
PaxDb; Q13057; -.
PeptideAtlas; Q13057; -.
PRIDE; Q13057; -.
DNASU; 80347; -.
Ensembl; ENST00000393818; ENSP00000377406; ENSG00000068120. [Q13057-1]
Ensembl; ENST00000421097; ENSP00000393564; ENSG00000068120. [Q13057-1]
Ensembl; ENST00000590958; ENSP00000464814; ENSG00000068120. [Q13057-2]
GeneID; 80347; -.
KEGG; hsa:80347; -.
UCSC; uc002hzz.5; human. [Q13057-1]
CTD; 80347; -.
DisGeNET; 80347; -.
EuPathDB; HostDB:ENSG00000068120.14; -.
GeneCards; COASY; -.
HGNC; HGNC:29932; COASY.
HPA; HPA022875; -.
HPA; HPA022912; -.
HPA; HPA023273; -.
MalaCards; COASY; -.
MIM; 609855; gene.
MIM; 615643; phenotype.
neXtProt; NX_Q13057; -.
OpenTargets; ENSG00000068120; -.
Orphanet; 397725; COASY protein-associated neurodegeneration.
PharmGKB; PA134867942; -.
eggNOG; KOG3220; Eukaryota.
eggNOG; KOG3351; Eukaryota.
eggNOG; COG0237; LUCA.
eggNOG; COG1019; LUCA.
GeneTree; ENSGT00550000075078; -.
HOVERGEN; HBG051059; -.
InParanoid; Q13057; -.
KO; K02318; -.
OMA; SRVFGNK; -.
OrthoDB; EOG091G053D; -.
PhylomeDB; Q13057; -.
BioCyc; MetaCyc:HS00931-MONOMER; -.
BRENDA; 2.7.1.24; 2681.
BRENDA; 2.7.7.3; 2681.
Reactome; R-HSA-196783; Coenzyme A biosynthesis.
SABIO-RK; Q13057; -.
UniPathway; UPA00241; UER00355.
UniPathway; UPA00241; UER00356.
ChiTaRS; COASY; human.
GeneWiki; COASY; -.
GenomeRNAi; 80347; -.
PRO; PR:Q13057; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000068120; -.
CleanEx; HS_COASY; -.
ExpressionAtlas; Q13057; baseline and differential.
Genevisible; Q13057; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004140; F:dephospho-CoA kinase activity; IDA:UniProtKB.
GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IDA:UniProtKB.
GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:UniProtKB.
GO; GO:0009108; P:coenzyme biosynthetic process; TAS:Reactome.
CDD; cd02022; DPCK; 1.
Gene3D; 3.40.50.620; -; 1.
HAMAP; MF_00376; Dephospho_CoA_kinase; 1.
InterPro; IPR004821; Cyt_trans-like.
InterPro; IPR001977; Depp_CoAkinase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF01121; CoaE; 1.
Pfam; PF01467; CTP_transf_like; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00152; TIGR00152; 1.
PROSITE; PS51219; DPCK; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Coenzyme A biosynthesis;
Complete proteome; Cytoplasm; Disease mutation; Kinase; Mitochondrion;
Multifunctional enzyme; Neurodegeneration; Nucleotide-binding;
Nucleotidyltransferase; Phosphoprotein; Polymorphism;
Reference proteome; Transferase.
CHAIN 1 564 Bifunctional coenzyme A synthase.
/FTId=PRO_0000173039.
DOMAIN 360 563 DPCK.
NP_BIND 365 372 ATP. {ECO:0000255}.
REGION 180 358 Phosphopantetheine adenylyltransferase.
MOD_RES 178 178 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 183 183 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 1 1 M -> MRTPRLRAQPRGAVYQAPSPPPAPVGLGSM (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036404.
VARIANT 55 55 S -> Y (in dbSNP:rs615942).
{ECO:0000269|PubMed:11923312,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.6}.
/FTId=VAR_030299.
VARIANT 499 499 R -> C (in NBIA6; dbSNP:rs140709867).
{ECO:0000269|PubMed:24360804}.
/FTId=VAR_070975.
CONFLICT 41 41 L -> P (in Ref. 4; BAG36775).
{ECO:0000305}.
SEQUENCE 564 AA; 62329 MW; 7DC9E93B356C5DB7 CRC64;
MAVFRSGLLV LTTPLASLAP RLASILTSAA RLVNHTLYVH LQPGMSLEGP AQPQSSPVQA
TFEVLDFITH LYAGADVHRH LDVRILLTNI RTKSTFLPPL PTSVQNLAHP PEVVLTDFQT
LDGSQYNPVK QQLVRYATSC YSCCPRLASV LLYSDYGIGE VPVEPLDVPL PSTIRPASPV
AGSPKQPVRG YYRGAVGGTF DRLHNAHKVL LSVACILAQE QLVVGVADKD LLKSKLLPEL
LQPYTERVEH LSEFLVDIKP SLTFDVIPLL DPYGPAGSDP SLEFLVVSEE TYRGGMAINR
FRLENDLEEL ALYQIQLLKD LRHTENEEDK VSSSSFRQRM LGNLLRPPYE RPELPTCLYV
IGLTGISGSG KSSIAQRLKG LGAFVIDSDH LGHRAYAPGG PAYQPVVEAF GTDILHKDGI
INRKVLGSRV FGNKKQLKIL TDIMWPIIAK LAREEMDRAV AEGKRVCVID AAVLLEAGWQ
NLVHEVWTAV IPETEAVRRI VERDGLSEAA AQSRLQSQMS GQQLVEQSHV VLSTLWEPHI
TQRQVEKAWA LLQKRIPKTH QALD


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