ID A0A0F2PGD2_9FIRM Unreviewed; 396 AA. AC A0A0F2PGD2; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 19-JAN-2022, entry version 19. DE RecName: Full=Coenzyme A biosynthesis bifunctional protein CoaBC {ECO:0000256|HAMAP-Rule:MF_02225}; DE AltName: Full=DNA/pantothenate metabolism flavoprotein {ECO:0000256|HAMAP-Rule:MF_02225}; DE AltName: Full=Phosphopantothenoylcysteine synthetase/decarboxylase {ECO:0000256|HAMAP-Rule:MF_02225}; DE Short=PPCS-PPCDC {ECO:0000256|HAMAP-Rule:MF_02225}; DE Includes: DE RecName: Full=Phosphopantothenoylcysteine decarboxylase {ECO:0000256|HAMAP-Rule:MF_02225}; DE Short=PPC decarboxylase {ECO:0000256|HAMAP-Rule:MF_02225}; DE Short=PPC-DC {ECO:0000256|HAMAP-Rule:MF_02225}; DE EC=4.1.1.36 {ECO:0000256|HAMAP-Rule:MF_02225}; DE AltName: Full=CoaC {ECO:0000256|HAMAP-Rule:MF_02225}; DE Includes: DE RecName: Full=Phosphopantothenate--cysteine ligase {ECO:0000256|HAMAP-Rule:MF_02225}; DE EC=6.3.2.5 {ECO:0000256|HAMAP-Rule:MF_02225}; DE AltName: Full=CoaB {ECO:0000256|HAMAP-Rule:MF_02225}; DE AltName: Full=Phosphopantothenoylcysteine synthetase {ECO:0000256|HAMAP-Rule:MF_02225}; DE Short=PPC synthetase {ECO:0000256|HAMAP-Rule:MF_02225}; DE Short=PPC-S {ECO:0000256|HAMAP-Rule:MF_02225}; GN Name=coaBC {ECO:0000256|HAMAP-Rule:MF_02225}; GN ORFNames=VR67_09810 {ECO:0000313|EMBL:KJS12461.1}; OS Peptococcaceae bacterium BRH_c8a. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae. OX NCBI_TaxID=1629715 {ECO:0000313|EMBL:KJS12461.1, ECO:0000313|Proteomes:UP000033493}; RN [1] {ECO:0000313|EMBL:KJS12461.1, ECO:0000313|Proteomes:UP000033493} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c8a {ECO:0000313|EMBL:KJS12461.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes two sequential steps in the biosynthesis of CC coenzyme A. In the first step cysteine is conjugated to 4'- CC phosphopantothenate to form 4-phosphopantothenoylcysteine. In the CC second step the latter compound is decarboxylated to form 4'- CC phosphopantotheine. {ECO:0000256|HAMAP-Rule:MF_02225}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-4'-phosphopantothenate + CTP + L-cysteine = CMP + CC diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine; CC Xref=Rhea:RHEA:19397, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:35235, ChEBI:CHEBI:37563, CC ChEBI:CHEBI:59458, ChEBI:CHEBI:60377; EC=6.3.2.5; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02225}; 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 Evidence={ECO:0000256|HAMAP-Rule:MF_02225}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02225}; CC Note=Binds 1 FMN per subunit. {ECO:0000256|HAMAP-Rule:MF_02225}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_02225}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)- CC pantothenate: step 2/5. {ECO:0000256|HAMAP-Rule:MF_02225}. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)- CC pantothenate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_02225}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PPC synthetase CC family. {ECO:0000256|HAMAP-Rule:MF_02225}. CC -!- SIMILARITY: In the N-terminal section; belongs to the HFCD (homo- CC oligomeric flavin containing Cys decarboxylase) superfamily. CC {ECO:0000256|HAMAP-Rule:MF_02225}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02225}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KJS12461.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LADP01000021; KJS12461.1; -; Genomic_DNA. DR STRING; 1629715.VR67_09810; -. DR EnsemblBacteria; KJS12461; KJS12461; VR67_09810. DR PATRIC; fig|1629715.3.peg.4316; -. DR UniPathway; UPA00241; UER00353. DR Proteomes; UP000033493; Unassembled WGS sequence. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0015941; P:pantothenate catabolic process; IEA:InterPro. DR Gene3D; 3.40.50.10300; -; 1. DR Gene3D; 3.40.50.1950; -; 1. DR HAMAP; MF_02225; CoaBC; 1. DR InterPro; IPR035929; CoaB-like_sf. DR InterPro; IPR005252; CoaBC. DR InterPro; IPR007085; DNA/pantothenate-metab_flavo_C. DR InterPro; IPR036551; Flavin_trans-like. DR InterPro; IPR003382; Flavoprotein. DR Pfam; PF04127; DFP; 1. DR Pfam; PF02441; Flavoprotein; 1. DR SUPFAM; SSF102645; SSF102645; 1. DR SUPFAM; SSF52507; SSF52507; 1. PE 3: Inferred from homology; KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP- KW Rule:MF_02225}; Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02225}; KW FMN {ECO:0000256|HAMAP-Rule:MF_02225}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02225}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02225}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02225}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02225}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_02225}. FT DOMAIN 6..177 FT /note="Flavoprotein" FT /evidence="ECO:0000259|Pfam:PF02441" FT DOMAIN 185..365 FT /note="DFP" FT /evidence="ECO:0000259|Pfam:PF04127" FT REGION 1..189 FT /note="Phosphopantothenoylcysteine decarboxylase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT REGION 190..396 FT /note="Phosphopantothenate--cysteine ligase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT ACT_SITE 157 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 278 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 288 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 321 FT /note="CTP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 335 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 339 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" SQ SEQUENCE 396 AA; 42796 MW; E7A33A76599AEE2B CRC64; MLVGKYIVVG VSGGIAAHRA LDLTSNLVKA GAEVHVIMTG AAREFIRPLA FEAISGHRVH YDIFAAPPGW RYPHLELARK ADLAVVAPAT ANIIAKLACG LADDLVTTAA LAMICPLVIC PAMNLYMYRN PVVQENLERL RRRGVSIIDP ASGRQACGDE GPGRLAEVSV IVQQIEHLLG TNQDLAGLKV LVTAGGTCEP IDPVRYITNR SSGKMGYALA KTAAVRGAKV YLVSAPTRLV PPTGIEMVNV ETAEQMYRAV MDLYPQMDAV VKAAAVSDYR PGKYQDQKIK KGGGLVLELE RTRDILSELG NQKKNQVLVG FAAETQDLVQ NATDKLVKKN LDLLVANDVT QTGAGFGTDT NIVKLLYPNG RVESLPIMDK LEISHRIWDE VIKIRG //