ID A0A1F4CY57_9PROT Unreviewed; 397 AA. AC A0A1F4CY57; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 28-MAR-2018, entry version 13. 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=A3G26_04845 {ECO:0000313|EMBL:OGA41659.1}; OS Betaproteobacteria bacterium RIFCSPLOWO2_12_FULL_65_110. OC Bacteria; Proteobacteria; Betaproteobacteria. OX NCBI_TaxID=1797500 {ECO:0000313|EMBL:OGA41659.1, ECO:0000313|Proteomes:UP000176596}; RN [1] {ECO:0000313|EMBL:OGA41659.1, ECO:0000313|Proteomes:UP000176596} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=27774985; DOI=10.1038/ncomms13219; RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J., RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., RA Brodie E.L., Williams K.H., Hubbard S.S., Banfield J.F.; RT "Thousands of microbial genomes shed light on interconnected RT biogeochemical processes in an aquifer system."; RL Nat. Commun. 7:13219-13219(2016). 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: CTP + (R)-4'-phosphopantothenate + L-cysteine CC = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine. CC {ECO:0000256|RuleBase:RU364078}. CC -!- CATALYTIC ACTIVITY: N-((R)-4'-phosphopantothenoyl)-L-cysteine = CC pantotheine 4'-phosphate + CO(2). {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:OGA41659.1}. 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; MERL01000079; OGA41659.1; -; Genomic_DNA. DR UniPathway; UPA00241; UER00353. DR Proteomes; UP000176596; Unassembled WGS sequence. 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:UP000176596}; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000176596}. FT DOMAIN 7 180 Flavoprotein. {ECO:0000259|Pfam:PF02441}. FT DOMAIN 186 365 DFP. {ECO:0000259|Pfam:PF04127}. SQ SEQUENCE 397 AA; 41796 MW; D8BDFE33864DDD83 CRC64; MTELAGKRIL LGLTGGIAAY KAGELARLFV RSGADVQVVM TRAACGFVTP ATMQALSGKP VYTDMWDGRI PNNMGHIELS RDRDLIVVAP ASADFMAKLA NGLADDLLSA LCLARRSPLA VAPAMNVEMW NHPATQRNAA QLRADGVAIL GPASGDQACG ETGMGRMLEA AEIYAEAVRA LSPKVLEGKR VLVTAGPTYE PIDTVRGITN QSSGKMGYAV AQAAAEAGAQ VTLVSGRTAL PTPAAVERVD VVTAREMHDA VMARVKRTDV FIAVAAVADY HVVNARGQKI KRSAGNPKIE LAPNPDILGA VAAGKSAPFC VGFAAETENL KAYAQDKRHQ KGIPLLAANL AQEAFGRDDN ALTLFDDAGE HVLARAPKIV LARQLVAHIA RMLPKAR //