ID S4YCX1_SORCE Unreviewed; 437 AA. AC S4YCX1; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 13-NOV-2019, entry version 32. 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=SCE1572_42935 {ECO:0000313|EMBL:AGP40663.1}; OS Sorangium cellulosum So0157-2. OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Sorangiineae; Polyangiaceae; Sorangium. OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP40663.1, ECO:0000313|Proteomes:UP000014803}; RN [1] {ECO:0000313|EMBL:AGP40663.1, ECO:0000313|Proteomes:UP000014803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP40663.1, RC ECO:0000313|Proteomes:UP000014803}; RX PubMed=23812535; DOI=10.1038/srep02101; RA Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G., RA Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.; RT "Extraordinary expansion of a Sorangium cellulosum genome from an RT alkaline milieu."; RL Sci. Rep. 3:2101-2101(2013). 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 --------------------------------------------------------------------------- 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; CP003969; AGP40663.1; -; Genomic_DNA. DR STRING; 1254432.SCE1572_42935; -. DR EnsemblBacteria; AGP40663; AGP40663; SCE1572_42935. DR KEGG; scu:SCE1572_42935; -. DR PATRIC; fig|1254432.3.peg.9712; -. DR KO; K13038; -. DR OrthoDB; 1346419at2; -. DR BioCyc; SCEL1254432:SCE1572_RS44150-MONOMER; -. DR UniPathway; UPA00241; UER00353. DR Proteomes; UP000014803; Chromosome. 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 Complete proteome {ECO:0000313|Proteomes:UP000014803}; KW Decarboxylase {ECO:0000256|RuleBase:RU364078}; KW Flavoprotein {ECO:0000256|RuleBase:RU364078}; KW FMN {ECO:0000256|RuleBase:RU364078}; KW Ligase {ECO:0000256|RuleBase:RU364078}; KW Lyase {ECO:0000256|RuleBase:RU364078}. FT DOMAIN 32 202 Flavoprotein. {ECO:0000259|Pfam:PF02441}. FT DOMAIN 209 407 DFP. {ECO:0000259|Pfam:PF04127}. FT REGION 1 26 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. SQ SEQUENCE 437 AA; 44875 MW; 77A4FA409958EFA1 CRC64; MSGRTPSSPA PHPDAPAPPA AGHTAAGGRP TVALAVSGSI AAYKAAEVAR LLIQGGARVL PIMTRAAQQF LGPMTLSGLC GAPVRDTMWD PGFAGELHVA LAAEADLVLL VPATADVLAR LAAGRADDLV TALALCAKGP VLAAPAMHPR MWAHPATARN VATLEADGRV ELVGPVFGEV ASGERGLGRM AEPAAIAAAA LSRLGPRDLA GLRLVVTAGP TLEDLDPVRF LGNRSTGKMG FAVADRAALR GAQVTLIAGP VSLAAPPGAR RVDVRGALEM RAALWQALGE DLRGADALIM TAAVSDYRPA EQHATKLKRT PDLASLPLVP NPDLLAEVGL ARAGLDAAAR EGGARPPVLV GFAVETDSDD GVIAYARRKL ASKRVDMIVA NHAADSFGRD DNRATIVTRD AADALGVLPK PVLADRILDR VVQLCAR //