ID A0A841BES0_9PSEU Unreviewed; 406 AA. AC A0A841BES0; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 24-JAN-2024, entry version 10. 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=HDA45_007159 {ECO:0000313|EMBL:MBB5857072.1}; OS Amycolatopsis umgeniensis. OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales; OC Pseudonocardiaceae; Amycolatopsis. OX NCBI_TaxID=336628 {ECO:0000313|EMBL:MBB5857072.1, ECO:0000313|Proteomes:UP000580861}; RN [1] {ECO:0000313|EMBL:MBB5857072.1, ECO:0000313|Proteomes:UP000580861} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45272 {ECO:0000313|EMBL:MBB5857072.1, RC ECO:0000313|Proteomes:UP000580861}; RA Klenk H.-P.; RT "Sequencing the genomes of 1000 actinobacteria strains."; RL Submitted (AUG-2020) 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 -!- FUNCTION: Catalyzes two steps in the biosynthesis of coenzyme A. In the CC first step cysteine is conjugated to 4'-phosphopantothenate to form 4- CC phosphopantothenoylcysteine, in the latter compound is decarboxylated CC to form 4'-phosphopantotheine. {ECO:0000256|RuleBase:RU364078}. 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 ECO:0000256|RuleBase:RU364078}; 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 ECO:0000256|RuleBase:RU364078}; 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 ECO:0000256|RuleBase:RU364078}. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)- CC pantothenate: step 3/5. {ECO:0000256|HAMAP-Rule:MF_02225, CC ECO:0000256|RuleBase:RU364078}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PPC synthetase CC family. {ECO:0000256|HAMAP-Rule:MF_02225, CC ECO:0000256|RuleBase:RU364078}. 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, ECO:0000256|RuleBase:RU364078}. 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:MBB5857072.1}. 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; JACHMX010000001; MBB5857072.1; -; Genomic_DNA. DR AlphaFoldDB; A0A841BES0; -. DR UniPathway; UPA00241; UER00353. DR Proteomes; UP000580861; 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; CoaB-like; 1. DR Gene3D; 3.40.50.1950; Flavin prenyltransferase-like; 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 NCBIfam; TIGR00521; coaBC_dfp; 1. DR PANTHER; PTHR14359; HOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY; 1. DR PANTHER; PTHR14359:SF6; PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE; 1. DR Pfam; PF04127; DFP; 1. DR Pfam; PF02441; Flavoprotein; 1. DR SUPFAM; SSF102645; CoaB-like; 1. DR SUPFAM; SSF52507; Homo-oligomeric flavin-containing Cys decarboxylases, HFCD; 1. PE 3: Inferred from homology; KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP- KW Rule:MF_02225}; KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02225, KW ECO:0000256|RuleBase:RU364078}; KW FMN {ECO:0000256|HAMAP-Rule:MF_02225, ECO:0000256|RuleBase:RU364078}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02225, ECO:0000256|RuleBase:RU364078}; 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 5..171 FT /note="Flavoprotein" FT /evidence="ECO:0000259|Pfam:PF02441" FT DOMAIN 186..374 FT /note="DNA/pantothenate metabolism flavoprotein C-terminal" FT /evidence="ECO:0000259|Pfam:PF04127" FT REGION 1..190 FT /note="Phosphopantothenoylcysteine decarboxylase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT REGION 191..406 FT /note="Phosphopantothenate--cysteine ligase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 280 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 290 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 327 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 345 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 349 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" SQ SEQUENCE 406 AA; 42513 MW; 21F471BDD5CF0364 CRC64; MNKPKVVLGV GGGIAAYKAC EVLRGLTESG HDVRVVPTEA ALNFVGAATF EALSGNPVHT GVFTEVPDVQ HVRVGKEADL VIVVPATANL LAKAAHGIAD DLLTNTLLTA RCPVAFFPAM HTEMWEHPAT RDNVALLRSR GLVVAEPAAG RLTGKDTGKG RLADPAEIVD LARLLLAVPN ALPRDLEGVR VAISAGGTRE PLDPVRYLGN RSSGKQGYAL ARVAAQRGAE VTLVTAHTIA LPDPAGAKVV HVSTAEELRQ AMHAEAASAD VVVMAAAVAD FRPSNRAEHK IKKSDDTPDP VVELARNADI LAELVRNRSE GRLVVGFAAE TGDDKGGVLD HARVKLKRKG ADLLVVNAVG EGKAFGTEDN SGWLLGADGT EIPIPLGAKA ELASTLWDAV VTLMKR //