ID A0A417HQJ6_9CLOT Unreviewed; 397 AA. AC A0A417HQJ6; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 12-AUG-2020, entry version 6. DE RecName: Full=Coenzyme A biosynthesis bifunctional protein CoaBC {ECO:0000256|RuleBase:RU364078}; DE EC=4.1.1.36 {ECO:0000256|RuleBase:RU364078}; DE EC=6.3.2.5 {ECO:0000256|RuleBase:RU364078}; DE AltName: Full=DNA/pantothenate metabolism flavoprotein {ECO:0000256|RuleBase:RU364078}; GN Name=coaBC {ECO:0000313|EMBL:RHT74651.1}; GN ORFNames=DW742_10090 {ECO:0000313|EMBL:RHT74651.1}; OS Butyricicoccus sp. AM28-25. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Butyricicoccus; unclassified Butyricicoccus. OX NCBI_TaxID=2292294 {ECO:0000313|EMBL:RHT74651.1, ECO:0000313|Proteomes:UP000283242}; RN [1] {ECO:0000313|EMBL:RHT74651.1, ECO:0000313|Proteomes:UP000283242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM28-25 {ECO:0000313|EMBL:RHT74651.1, RC ECO:0000313|Proteomes:UP000283242}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut microbiota."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. 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|RuleBase:RU364078}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine = CO2 + D- CC pantetheine 4'-phosphate; 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|RuleBase:RU364078}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000256|RuleBase:RU364078}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)- CC pantothenate: step 2/5. {ECO:0000256|RuleBase:RU364078}. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)- CC pantothenate: step 3/5. {ECO:0000256|RuleBase:RU364078}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PPC synthetase CC family. {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|RuleBase:RU364078}. 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:RHT74651.1}. 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; QUJL01000011; RHT74651.1; -; Genomic_DNA. DR UniPathway; UPA00241; UER00353. DR Proteomes; UP000283242; Unassembled WGS sequence. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IEA:UniProtKB-EC. DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway. 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 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. DR TIGRFAMs; TIGR00521; coaBC_dfp; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, KW ECO:0000256|RuleBase:RU364078}; KW Flavoprotein {ECO:0000256|RuleBase:RU364078}; KW FMN {ECO:0000256|RuleBase:RU364078}; KW Ligase {ECO:0000256|RuleBase:RU364078, ECO:0000313|EMBL:RHT74651.1}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU364078, KW ECO:0000313|EMBL:RHT74651.1}. FT DOMAIN 6..173 FT /note="Flavoprotein" FT /evidence="ECO:0000259|Pfam:PF02441" FT DOMAIN 185..367 FT /note="DFP" FT /evidence="ECO:0000259|Pfam:PF04127" FT COILED 324..344 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 397 AA; 42466 MW; FA72CE0636E969DF CRC64; MRFAGKTVVL CVTGGIAAYK AADLTSKLHQ NGATVHVLMT ESATQFIAPM TFETLSGNRA VVDTFDRSFP WEVEHISLAK AADVFVIAPA TANVIAKAAH GIADDMVTTT LLATKAPVVV APAMNTGMYD NPVTQENLAA LRKRGFHIIE PDAGHLACGD SGRGKLPDTP TLLWGIEKAL TEQDLAGRHV LVTAGPTQEA MDPVRFLSNH STGKMGYAIA ARAAMRGADA TLVSGPTALD TPHGVTRVDI VSARDMYEAV TSRAPEQDFI IKAAAVGDYR PAQTADEKLK KGDGEMNIEL TRNPDILAAL GKDKKPGQLL CGFAMETQNL LDNAESKLRR KNCDMLVANS LRDKGAGFGT DTNVATLLFK DGHRETPPMM SKEELADLIL DRLLSMK //