ID A0A4R8GVM8_9FIRM Unreviewed; 399 AA. AC A0A4R8GVM8; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 16-OCT-2019, entry version 3. 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 ORFNames=C7959_1378 {ECO:0000313|EMBL:TDX46751.1}; OS Orenia marismortui. OC Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halobacteroidaceae; OC Orenia. OX NCBI_TaxID=46469 {ECO:0000313|EMBL:TDX46751.1, ECO:0000313|Proteomes:UP000295832}; RN [1] {ECO:0000313|EMBL:TDX46751.1, ECO:0000313|Proteomes:UP000295832} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSL 6dP {ECO:0000313|EMBL:TDX46751.1, RC ECO:0000313|Proteomes:UP000295832}; RA Wrighton K.; RT "Subsurface microbial communities from deep shales in Ohio and West RT Virginia, USA."; RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes two steps in the biosynthesis of coenzyme A. CC In the first step cysteine is conjugated to 4'-phosphopantothenate CC to form 4-phosphopantothenoylcysteine, in the latter compound is CC decarboxylated to form 4'-phosphopantotheine. CC {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 + CC D-pantetheine 4'-phosphate; Xref=Rhea:RHEA:16793, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:59458, CC 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 CC (R)-pantothenate: step 2/5. {ECO:0000256|RuleBase:RU364078}. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 3/5. {ECO:0000256|RuleBase:RU364078}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PPC CC synthetase 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 CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:TDX46751.1}. 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; SOEG01000037; TDX46751.1; -; Genomic_DNA. DR UniPathway; UPA00241; UER00353. DR Proteomes; UP000295832; Unassembled WGS sequence. 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 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 Complete proteome {ECO:0000313|Proteomes:UP000295832}; KW Decarboxylase {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:TDX46751.1}; KW Lyase {ECO:0000256|RuleBase:RU364078}; KW Reference proteome {ECO:0000313|Proteomes:UP000295832}. FT DOMAIN 5 175 Flavoprotein. {ECO:0000259|Pfam:PF02441}. FT DOMAIN 187 368 DFP. {ECO:0000259|Pfam:PF04127}. FT COILED 324 344 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 399 AA; 43582 MW; 7E46933072294C62 CRC64; MLEGKNVVIG VTGGIAVYKS VEIVSRLKKL GADVYVIMTK SATEFVKPMT FQSLSHNPVV VEMFGRAQYW DVEHISLADK ADLMLIAPAT ANIVGKIANG IADDMLSTTV MATQAPVVLC PAMNVNMYSN SIFQDNLSYL REKDYKIIEA DAGYLACGYE GRGRLSKPLE IVETSIAYLL APEEDLNDRK VLITAGGTME ALDPVRYLGN HSSGKMGYAL ARIAQARGAD VTLISAPTTL NDPKGVKKIE VRTAAEMEEM VLKYKAEQDI IIMAAAVADY RPKDYSDNKI KKESGDLVIR LERTEDILAK LGKDKDNQIL VGFAAESDNL VENAKDKLAR KNADLIVAND ITSADTGFAA DNNKVIIISK DREVDIPKAS KLEVAKQIID QICEMILNN //