ID S4YCX1_SORCE Unreviewed; 437 AA. AC S4YCX1; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 02-DEC-2020, entry version 37. 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=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 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 = 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|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 --------------------------------------------------------------------------- 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 eggNOG; COG0452; Bacteria. DR HOGENOM; CLU_033319_0_1_7; -. 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: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; -; 1. DR Gene3D; 3.40.50.1950; -; 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 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|ARBA:ARBA00022793, ECO:0000256|HAMAP- KW Rule:MF_02225, ECO:0000256|RuleBase:RU364078}; 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 ECO:0000256|RuleBase:RU364078}; 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 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 NP_BIND 332..335 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT REGION 1..213 FT /note="Phosphopantothenoylcysteine decarboxylase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 214..437 FT /note="Phosphopantothenate--cysteine ligase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 306 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 316 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 362 FT /note="CTP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 379 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 383 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" 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 //