COAC_DICDI
ID COAC_DICDI Reviewed; 197 AA.
AC Q54Y51;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Putative phosphopantothenoylcysteine decarboxylase;
DE Short=PPC-DC;
DE EC=4.1.1.36;
GN Name=ppcdc; ORFNames=DDB_G0278413;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Necessary for the biosynthesis of coenzyme A. Catalyzes the
CC decarboxylation of 4-phosphopantothenoylcysteine to form 4'-
CC phosphopantotheine (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine = (R)-4'-
CC phosphopantetheine + CO2; Xref=Rhea:RHEA:16793, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:59458, ChEBI:CHEBI:61723; EC=4.1.1.36;
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC Note=Binds 1 FMN per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 3/5.
CC -!- SUBUNIT: Homotrimer. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the HFCD (homooligomeric flavin containing Cys
CC decarboxylase) superfamily. {ECO:0000305}.
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DR EMBL; AAFI02000023; EAL68379.1; -; Genomic_DNA.
DR RefSeq; XP_642351.1; XM_637259.1.
DR AlphaFoldDB; Q54Y51; -.
DR SMR; Q54Y51; -.
DR STRING; 44689.DDB0231515; -.
DR PaxDb; Q54Y51; -.
DR EnsemblProtists; EAL68379; EAL68379; DDB_G0278413.
DR GeneID; 8621556; -.
DR KEGG; ddi:DDB_G0278413; -.
DR dictyBase; DDB_G0278413; ppcdc.
DR eggNOG; KOG0672; Eukaryota.
DR HOGENOM; CLU_033319_3_2_1; -.
DR InParanoid; Q54Y51; -.
DR OMA; NTRMYDH; -.
DR PhylomeDB; Q54Y51; -.
DR Reactome; R-DDI-196783; Coenzyme A biosynthesis.
DR UniPathway; UPA00241; UER00354.
DR PRO; PR:Q54Y51; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0071513; C:phosphopantothenoylcysteine decarboxylase complex; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; ISS:dictyBase.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; ISS:dictyBase.
DR Gene3D; 3.40.50.1950; -; 1.
DR InterPro; IPR036551; Flavin_trans-like.
DR InterPro; IPR003382; Flavoprotein.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
PE 3: Inferred from homology;
KW Coenzyme A biosynthesis; Decarboxylase; Flavoprotein; FMN; Lyase;
KW Reference proteome.
FT CHAIN 1..197
FT /note="Putative phosphopantothenoylcysteine decarboxylase"
FT /id="PRO_0000367258"
FT ACT_SITE 174
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 102..105
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 197 AA; 22383 MW; 665B8A1A3C726B04 CRC64;
MTITINNYNN DKKNLILGLT GSVATIKAKL LVEQLIQHFN LIVIPTETSL KFLSDQDFEF
ISSKCKIYKD KDEWENVDLL KRSALHIDLR NWANSILISP CSANTLGKIS NGLCDNLLTS
LIRAWDYKNK SMILAPAMNT MMWENPFTFK HIETLKSISP NVFIIDPIEK KLFCGDIGMG
AMEQVPKIVD FTINNLK
