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Coenzyme A biosynthesis bifunctional protein CoaBC (DNA/pantothenate metabolism flavoprotein) [Includes: Phosphopantothenoylcysteine decarboxylase (PPCDC) (EC 4.1.1.36) (CoaC); Phosphopantothenate--cysteine ligase (EC 6.3.2.5) (CoaB) (PPC synthetase) (PPCS) (Phosphopantothenoylcysteine synthase)]

 COABC_ECOLI             Reviewed;         406 AA.
P0ABQ0; P24285; P76718; Q2M7V3;
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 101.
RecName: Full=Coenzyme A biosynthesis bifunctional protein CoaBC;
AltName: Full=DNA/pantothenate metabolism flavoprotein;
Includes:
RecName: Full=Phosphopantothenoylcysteine decarboxylase;
Short=PPCDC;
EC=4.1.1.36 {ECO:0000269|PubMed:10922366};
AltName: Full=CoaC;
Includes:
RecName: Full=Phosphopantothenate--cysteine ligase;
EC=6.3.2.5 {ECO:0000269|PubMed:11278255};
AltName: Full=CoaB;
AltName: Full=PPC synthetase;
Short=PPCS;
AltName: Full=Phosphopantothenoylcysteine synthase;
Name=coaBC {ECO:0000303|PubMed:11278255};
Synonyms=dfp {ECO:0000303|PubMed:10922366};
OrderedLocusNames=b3639, JW5642;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=7686882; DOI=10.1006/geno.1993.1230;
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
"DNA sequence and analysis of 136 kilobases of the Escherichia coli
genome: organizational symmetry around the origin of replication.";
Genomics 16:551-561(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
PROTEIN SEQUENCE OF 2-11, CHARACTERIZATION OF COAC ACTIVITY, AND
MUTAGENESIS OF PHE-46; HIS-75; PRO-89; THR-91; MET-124; ASN-125 AND
MET-128.
PubMed=10922366; DOI=10.1074/jbc.M004273200;
Kupke T., Uebele M., Schmid D., Jung G., Blaesse M., Steinbacher S.;
"Molecular characterization of lantibiotic-synthesizing enzyme EpiD
reveals a function for bacterial Dfp proteins in coenzyme A
biosynthesis.";
J. Biol. Chem. 275:31838-31846(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 288-406.
STRAIN=K12;
PubMed=6139280;
Lundberg L.G., Thoresson H.-O., Karlstroem O.H., Nyman P.O.;
"Nucleotide sequence of the structural gene for dUTPase of Escherichia
coli K-12.";
EMBO J. 2:967-971(1983).
[6]
CHARACTERIZATION OF COAB ACTIVITY.
PubMed=11278255; DOI=10.1074/jbc.C100033200;
Strauss E., Kinsland C., Ge Y., McLafferty F.W., Begley T.P.;
"Phosphopantothenoylcysteine synthetase from Escherichia coli.
Identification and characterization of the last unidentified coenzyme
A biosynthetic enzyme in bacteria.";
J. Biol. Chem. 276:13513-13516(2001).
[7]
CHARACTERIZATION OF COAC ACTIVITY, AND MUTAGENESIS OF GLY-11; GLY-14;
GLY-15; ILE-16; ALA-17; TYR-19; LYS-20 AND ASN-125.
PubMed=11358972; DOI=10.1074/jbc.M103342200;
Kupke T.;
"Molecular characterization of the 4'-phosphopantothenoylcysteine
decarboxylase domain of bacterial Dfp flavoproteins.";
J. Biol. Chem. 276:27597-27604(2001).
[8]
CHARACTERIZATION OF COAB ACTIVITY, AND MUTAGENESIS OF THR-194;
THR-198; ASP-203; ASN-210; SER-212; LYS-215; ALA-275; LYS-289; LYS-291
AND LYS-292.
PubMed=12140293; DOI=10.1074/jbc.M206188200;
Kupke T.;
"Molecular characterization of the 4'-phosphopantothenoylcysteine
synthetase domain of bacterial dfp flavoproteins.";
J. Biol. Chem. 277:36137-36145(2002).
[9]
CHARACTERIZATION OF COAB ACTIVITY, AND MUTAGENESIS OF ASN-210 AND
ALA-275.
PubMed=14686929; DOI=10.1046/j.1432-1033.2003.03916.x;
Kupke T.;
"Active-site residues and amino acid specificity of the bacterial 4'-
phosphopantothenoylcysteine synthetase CoaB.";
Eur. J. Biochem. 271:163-172(2004).
[10] {ECO:0000244|PDB:1U7U, ECO:0000244|PDB:1U7W, ECO:0000244|PDB:1U7Z, ECO:0000244|PDB:1U80}
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 181-406 OF MUTANT ASP-210
APOENZYME AND OF COMPLEX WITH SUBSTRATE; CTP AND CALCIUM IONS.
PubMed=15530362; DOI=10.1016/j.str.2004.08.007;
Stanitzek S., Augustin M.A., Huber R., Kupke T., Steinbacher S.;
"Structural basis of CTP-dependent peptide bond formation in coenzyme
A biosynthesis catalyzed by Escherichia coli PPC synthetase.";
Structure 12:1977-1988(2004).
-!- FUNCTION: Catalyzes two steps in the biosynthesis of coenzyme A.
In the first step cysteine is conjugated to 4'-phosphopantothenate
to form 4-phosphopantothenoylcysteine (PubMed:11278255). In the
second the latter compound is decarboxylated to form 4'-
phosphopantotheine (PubMed:10922366).
{ECO:0000269|PubMed:10922366, ECO:0000269|PubMed:11278255}.
-!- CATALYTIC ACTIVITY: N-((R)-4'-phosphopantothenoyl)-L-cysteine =
pantotheine 4'-phosphate + CO(2). {ECO:0000269|PubMed:10922366}.
-!- CATALYTIC ACTIVITY: CTP + (R)-4'-phosphopantothenate + L-cysteine
= CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine.
{ECO:0000269|PubMed:11278255}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Note=Binds 1 FMN per subunit.;
-!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
(R)-pantothenate: step 2/5. {ECO:0000269|PubMed:11278255}.
-!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
(R)-pantothenate: step 3/5. {ECO:0000269|PubMed:10922366}.
-!- SUBUNIT: Homododecamer, the CoaB domains form homodimers.
-!- INTERACTION:
P0A7L0:rplA; NbExp=2; IntAct=EBI-548929, EBI-543771;
P0A7Z4:rpoA; NbExp=2; IntAct=EBI-548929, EBI-544985;
-!- SIMILARITY: In the N-terminal section; belongs to the HFCD (homo-
oligomeric flavin containing Cys decarboxylase) superfamily.
{ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the PPC
synthetase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA61992.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; L10328; AAA61992.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC76663.2; -; Genomic_DNA.
EMBL; AP009048; BAE77653.1; -; Genomic_DNA.
EMBL; V01578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_418096.4; NC_000913.3.
RefSeq; WP_000050139.1; NZ_LN832404.1.
PDB; 1U7U; X-ray; 2.40 A; A=181-406.
PDB; 1U7W; X-ray; 2.50 A; A/B/C=181-406.
PDB; 1U7Z; X-ray; 2.30 A; A/B/C=181-406.
PDB; 1U80; X-ray; 2.85 A; A/B/C=181-406.
PDBsum; 1U7U; -.
PDBsum; 1U7W; -.
PDBsum; 1U7Z; -.
PDBsum; 1U80; -.
ProteinModelPortal; P0ABQ0; -.
SMR; P0ABQ0; -.
DIP; DIP-48472N; -.
IntAct; P0ABQ0; 2.
STRING; 316385.ECDH10B_3821; -.
DrugBank; DB03403; Cytidine-5'-Monophosphate.
DrugBank; DB02431; Cytidine-5'-Triphosphate.
PaxDb; P0ABQ0; -.
PRIDE; P0ABQ0; -.
EnsemblBacteria; AAC76663; AAC76663; b3639.
EnsemblBacteria; BAE77653; BAE77653; BAE77653.
GeneID; 949047; -.
KEGG; ecj:JW5642; -.
KEGG; eco:b3639; -.
PATRIC; fig|1411691.4.peg.3067; -.
EchoBASE; EB0004; -.
EcoGene; EG10004; dfp.
eggNOG; ENOG4105CJS; Bacteria.
eggNOG; COG0452; LUCA.
HOGENOM; HOG000037526; -.
InParanoid; P0ABQ0; -.
KO; K13038; -.
PhylomeDB; P0ABQ0; -.
BioCyc; EcoCyc:EG10004-MONOMER; -.
BioCyc; MetaCyc:EG10004-MONOMER; -.
BRENDA; 6.3.2.5; 2026.
SABIO-RK; P0ABQ0; -.
UniPathway; UPA00241; UER00353.
UniPathway; UPA00241; UER00354.
EvolutionaryTrace; P0ABQ0; -.
PRO; PR:P0ABQ0; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IDA:EcoCyc.
GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IDA:EcoCyc.
GO; GO:0015937; P:coenzyme A biosynthetic process; IDA:EcoCyc.
GO; GO:0015941; P:pantothenate catabolic process; IEA:InterPro.
Gene3D; 3.40.50.10300; -; 1.
Gene3D; 3.40.50.1950; -; 1.
InterPro; IPR035929; CoaB-like_sf.
InterPro; IPR005252; CoaBC.
InterPro; IPR007085; DNA/pantothenate-metab_flavo_C.
InterPro; IPR036551; Flavin_trans-like.
InterPro; IPR003382; Flavoprotein.
Pfam; PF04127; DFP; 1.
Pfam; PF02441; Flavoprotein; 1.
SUPFAM; SSF102645; SSF102645; 1.
SUPFAM; SSF52507; SSF52507; 1.
TIGRFAMs; TIGR00521; coaBC_dfp; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Decarboxylase;
Direct protein sequencing; Flavoprotein; FMN; Ligase; Lyase;
Magnesium; Metal-binding; Multifunctional enzyme; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10922366}.
CHAIN 2 406 Coenzyme A biosynthesis bifunctional
protein CoaBC.
/FTId=PRO_0000182022.
NP_BIND 273 275 CTP. {ECO:0000244|PDB:1U7W,
ECO:0000269|PubMed:15530362}.
NP_BIND 308 311 CTP. {ECO:0000244|PDB:1U7W,
ECO:0000269|PubMed:15530362}.
REGION 2 188 Phosphopantothenoylcysteine
decarboxylase.
REGION 189 406 Phosphopantothenate--cysteine ligase.
ACT_SITE 158 158 Proton donor. {ECO:0000305}.
BINDING 125 125 Substrate. {ECO:0000250}.
BINDING 279 279 CTP. {ECO:0000244|PDB:1U7W,
ECO:0000269|PubMed:15530362}.
BINDING 289 289 CTP. {ECO:0000244|PDB:1U7W,
ECO:0000269|PubMed:15530362}.
BINDING 327 327 CTP; via amide nitrogen.
{ECO:0000244|PDB:1U7W,
ECO:0000269|PubMed:15530362}.
BINDING 341 341 CTP. {ECO:0000244|PDB:1U7W,
ECO:0000269|PubMed:15530362}.
BINDING 345 345 CTP. {ECO:0000244|PDB:1U7W,
ECO:0000269|PubMed:15530362}.
MUTAGEN 11 11 G->D: In Dfp-707; temperature-sensitive,
impairs folding.
{ECO:0000269|PubMed:11358972}.
MUTAGEN 14 14 G->S: No FMN binding.
{ECO:0000269|PubMed:11358972}.
MUTAGEN 15 15 G->A: Less than 5% of wild-type activity.
{ECO:0000269|PubMed:11358972}.
MUTAGEN 16 16 I->L: Severely reduced activity.
{ECO:0000269|PubMed:11358972}.
MUTAGEN 16 16 I->V: Slightly reduced activity.
{ECO:0000269|PubMed:11358972}.
MUTAGEN 17 17 A->D: Less than 5% of wild-type activity.
{ECO:0000269|PubMed:11358972}.
MUTAGEN 17 17 A->G,S: Almost wild-type activity.
{ECO:0000269|PubMed:11358972}.
MUTAGEN 19 19 Y->F: Almost wild-type activity.
{ECO:0000269|PubMed:11358972}.
MUTAGEN 19 19 Y->L: Reduced activity.
{ECO:0000269|PubMed:11358972}.
MUTAGEN 20 20 K->N,Q: Reduced activity.
{ECO:0000269|PubMed:11358972}.
MUTAGEN 20 20 K->R: Almost wild-type activity.
{ECO:0000269|PubMed:11358972}.
MUTAGEN 46 46 F->L: Reduced activity.
{ECO:0000269|PubMed:10922366}.
MUTAGEN 75 75 H->N: Loss of activity.
{ECO:0000269|PubMed:10922366}.
MUTAGEN 89 89 P->A: Binds FMN, but more loosely than
wild-type. {ECO:0000269|PubMed:10922366}.
MUTAGEN 89 89 P->D: No FMN binding.
{ECO:0000269|PubMed:10922366}.
MUTAGEN 91 91 T->V: Binds FMN.
{ECO:0000269|PubMed:10922366}.
MUTAGEN 124 124 M->L: No effect.
{ECO:0000269|PubMed:10922366}.
MUTAGEN 125 125 N->D,Q: Loss of activity.
{ECO:0000269|PubMed:10922366,
ECO:0000269|PubMed:11358972}.
MUTAGEN 128 128 M->L: Severely reduced activity.
{ECO:0000269|PubMed:10922366}.
MUTAGEN 158 158 C->A,S: Loss of activity.
MUTAGEN 194 194 T->V: Loss of dimerization.
{ECO:0000269|PubMed:12140293}.
MUTAGEN 198 198 T->V: Loss of dimerization.
{ECO:0000269|PubMed:12140293}.
MUTAGEN 203 203 D->N: Loss of dimerization.
{ECO:0000269|PubMed:12140293}.
MUTAGEN 210 210 N->D: Loss of activity, reaction
intermediate detectable.
{ECO:0000269|PubMed:12140293,
ECO:0000269|PubMed:14686929}.
MUTAGEN 210 210 N->H,K: Loss of activity, reaction
intermediate not detectable.
{ECO:0000269|PubMed:12140293,
ECO:0000269|PubMed:14686929}.
MUTAGEN 212 212 S->A: Small effect on activity.
{ECO:0000269|PubMed:12140293}.
MUTAGEN 215 215 K->Q: No effect.
{ECO:0000269|PubMed:12140293}.
MUTAGEN 275 275 A->V: Loss of dimerization.
{ECO:0000269|PubMed:12140293,
ECO:0000269|PubMed:14686929}.
MUTAGEN 289 289 K->Q: Loss of activity.
{ECO:0000269|PubMed:12140293}.
MUTAGEN 291 291 K->Q: Reduced activity.
{ECO:0000269|PubMed:12140293}.
MUTAGEN 292 292 K->Q: Small effect on activity.
{ECO:0000269|PubMed:12140293}.
TURN 185 188 {ECO:0000244|PDB:1U7Z}.
STRAND 190 197 {ECO:0000244|PDB:1U7Z}.
STRAND 199 210 {ECO:0000244|PDB:1U7Z}.
HELIX 215 226 {ECO:0000244|PDB:1U7Z}.
STRAND 230 235 {ECO:0000244|PDB:1U7Z}.
STRAND 246 250 {ECO:0000244|PDB:1U7Z}.
HELIX 254 264 {ECO:0000244|PDB:1U7Z}.
HELIX 265 267 {ECO:0000244|PDB:1U7Z}.
STRAND 269 273 {ECO:0000244|PDB:1U7Z}.
STRAND 279 284 {ECO:0000244|PDB:1U7Z}.
STRAND 299 306 {ECO:0000244|PDB:1U7Z}.
HELIX 310 316 {ECO:0000244|PDB:1U7Z}.
STRAND 318 320 {ECO:0000244|PDB:1U7Z}.
STRAND 323 333 {ECO:0000244|PDB:1U7Z}.
HELIX 334 345 {ECO:0000244|PDB:1U7Z}.
STRAND 348 354 {ECO:0000244|PDB:1U7Z}.
STRAND 364 373 {ECO:0000244|PDB:1U7Z}.
STRAND 376 384 {ECO:0000244|PDB:1U7Z}.
HELIX 385 403 {ECO:0000244|PDB:1U7Z}.
SEQUENCE 406 AA; 43438 MW; CBD11B9347E8C6AB CRC64;
MSLAGKKIVL GVSGGIAAYK TPELVRRLRD RGADVRVAMT EAAKAFITPL SLQAVSGYPV
SDSLLDPAAE AAMGHIELGK WADLVILAPA TADLIARVAA GMANDLVSTI CLATPAPVAV
LPAMNQQMYR AAATQHNLEV LASRGLLIWG PDSGSQACGD IGPGRMLDPL TIVDMAVAHF
SPVNDLKHLN IMITAGPTRE PLDPVRYISN HSSGKMGFAI AAAAARRGAN VTLVSGPVSL
PTPPFVKRVD VMTALEMEAA VNASVQQQNI FIGCAAVADY RAATVAPEKI KKQATQGDEL
TIKMVKNPDI VAGVAALKDH RPYVVGFAAE TNNVEEYARQ KRIRKNLDLI CANDVSQPTQ
GFNSDNNALH LFWQDGDKVL PLERKELLGQ LLLDEIVTRY DEKNRR


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