ID S4YCX1_SORCE Unreviewed; 437 AA. AC S4YCX1; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 11-DEC-2019, entry version 33. 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; Sorangiineae; OC 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 alkaline RT milieu."; RL Sci. Rep. 3:2101-2101(2013). 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 --------------------------------------------------------------------------- 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 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 FT /note="Flavoprotein" FT /evidence="ECO:0000259|Pfam:PF02441" FT DOMAIN 209..407 FT /note="DFP" FT /evidence="ECO:0000259|Pfam:PF04127" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-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 //