ID   COAC_STRMU              Reviewed;         179 AA.
AC   Q54433;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Probable phosphopantothenoylcysteine decarboxylase;
DE            Short=PPCDC;
DE            EC=4.1.1.36;
GN   Name=coaC; OrderedLocusNames=SMU_1075;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-145.
RC   STRAIN=NG8;
RX   PubMed=8763945; DOI=10.1128/jb.178.14.4166-4175.1996;
RA   Gutierrez J.A., Crowley P.J., Brown D.P., Hillman J.D., Youngman P.,
RA   Bleiweis A.S.;
RT   "Insertional mutagenesis and recovery of interrupted genes of Streptococcus
RT   mutans by using transposon Tn917: preliminary characterization of mutants
RT   displaying acid sensitivity and nutritional requirements.";
RL   J. Bacteriol. 178:4166-4175(1996).
CC   -!- FUNCTION: Catalyzes the decarboxylation of 4'-
CC       phosphopantothenoylcysteine to 4'-phosphopantetheine.
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   -!- SIMILARITY: Belongs to the HFCD (homooligomeric flavin containing Cys
CC       decarboxylase) superfamily. {ECO:0000305}.
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DR   EMBL; AE014133; AAN58773.1; -; Genomic_DNA.
DR   EMBL; U48885; AAC44502.1; -; Genomic_DNA.
DR   RefSeq; NP_721467.1; NC_004350.2.
DR   RefSeq; WP_002262265.1; NC_004350.2.
DR   AlphaFoldDB; Q54433; -.
DR   SMR; Q54433; -.
DR   STRING; 210007.SMU_1075; -.
DR   EnsemblBacteria; AAN58773; AAN58773; SMU_1075.
DR   KEGG; smu:SMU_1075; -.
DR   PATRIC; fig|210007.7.peg.962; -.
DR   eggNOG; COG0452; Bacteria.
DR   HOGENOM; CLU_033319_2_0_9; -.
DR   OMA; NTRMYDH; -.
DR   PhylomeDB; Q54433; -.
DR   UniPathway; UPA00241; UER00354.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1950; -; 1.
DR   InterPro; IPR011847; CoaC_strep.
DR   InterPro; IPR036551; Flavin_trans-like.
DR   InterPro; IPR003382; Flavoprotein.
DR   Pfam; PF02441; Flavoprotein; 1.
DR   SUPFAM; SSF52507; SSF52507; 1.
DR   TIGRFAMs; TIGR02113; coaC_strep; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Flavoprotein; FMN; Lyase; Reference proteome.
FT   CHAIN           1..179
FT                   /note="Probable phosphopantothenoylcysteine decarboxylase"
FT                   /id="PRO_0000182029"
FT   ACT_SITE        157
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        35
FT                   /note="L -> F (in Ref. 2; AAC44502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85
FT                   /note="A -> P (in Ref. 2; AAC44502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="A -> T (in Ref. 2; AAC44502)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   179 AA;  19282 MW;  3DB29C34CAA399CB CRC64;
     MTKKILLAVS GSIAAYKAAD LSHQLTKLGY HVNVLMTNAA KQFIPPLTLQ VLSKNPVYSN
     VMKEDDPQVI NHIALAKQAD LFLLAPASAN TLAHLAHGFA DNIVTSVALA LPLEVPKFFA
     PAMNTKMYEN PITQSNIALL KKFGYKEIQP KSSVLACGDV GSGALADLDT IIQKIEEQL