ID A0A2Z5JVZ3_9ACTN Unreviewed; 423 AA. AC A0A2Z5JVZ3; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 05-DEC-2018, 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 Name=coaBC {ECO:0000313|EMBL:AXE84537.1}; GN ORFNames=C1703_05955 {ECO:0000313|EMBL:AXE84537.1}; OS Streptomyces sp. Go-475. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=2072505 {ECO:0000313|EMBL:AXE84537.1, ECO:0000313|Proteomes:UP000253251}; RN [1] {ECO:0000313|EMBL:AXE84537.1, ECO:0000313|Proteomes:UP000253251} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Go-475 {ECO:0000313|EMBL:AXE84537.1, RC ECO:0000313|Proteomes:UP000253251}; RX PubMed=29946312; DOI=.3389/fmicb.2018.01270; RA Kibret M., Guerrero-Garzon J.F., Urban E., Zehl M., Wronski V.K., RA Ruckert C., Busche T., Kalinowski J., Rollinger J.M., Abate D., RA Zotchev S.B.; RT "Streptomyces spp. From Ethiopia Producing Antimicrobial Compounds: RT Characterization via Bioassays, Genome Analyses, and Mass RT Spectrometry."; RL Front. Microbiol. 9:1270-1270(2018). 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; CP026121; AXE84537.1; -; Genomic_DNA. DR UniPathway; UPA00241; UER00353. DR Proteomes; UP000253251; 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:UP000253251}; 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 28 197 Flavoprotein. {ECO:0000259|Pfam:PF02441}. FT DOMAIN 208 392 DFP. {ECO:0000259|Pfam:PF04127}. SQ SEQUENCE 423 AA; 44373 MW; 73A8C2A328E55C8E CRC64; MESYGGPVAE ARVAEVQGET GSNVDKPKVV LGVSGGIAAY KACELLRRLT ESGHDVRVVP TASALHFVGA ATWSALSGKP VSTEVWDDVH EVPHVRIGQH ADLVVVAPAT ADLLAKAAHG LADDLLTNTL LTARCPVVFA PAMHTEMWEH PATQENVATL RRRGALVIEP AVGRLTGVDT GKGRLPDPAE IFEVCRRVLA RGVREPDLKG RHVVISAGGT REPLDPVRFL GNRSSGKQGY ALARTAAARG ARVTLIAANA TLPDPAGVDV VPVGTAVQLR EAVLKAAAEA DAVVMAAAVA DFRPATYAAG KIKKKDDQEP EPITLVRNPD ILAEVSADRA RAGQVVVGFA AETDDVLANG RAKLKRKGCD LLVVNEVGER KTFGSEENEA VVLGADGSET AVPHGPKEAL AETVWDLVAE RLG //