ID A0A0B7J466_PHOPO Unreviewed; 404 AA. AC A0A0B7J466; DT 01-APR-2015, integrated into UniProtKB/TrEMBL. DT 01-APR-2015, sequence version 1. DT 11-DEC-2019, entry version 19. 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=coaC {ECO:0000313|EMBL:CEO37856.1}; GN ORFNames=PPBDW_I10207 {ECO:0000313|EMBL:CEO37856.1}; OS Photobacterium phosphoreum ANT-2200. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Photobacterium. OX NCBI_TaxID=1454202 {ECO:0000313|EMBL:CEO37856.1, ECO:0000313|Proteomes:UP000019762}; RN [1] {ECO:0000313|EMBL:CEO37856.1, ECO:0000313|Proteomes:UP000019762} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ANT220 {ECO:0000313|Proteomes:UP000019762}; RA Genoscope - CEA; RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases. 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:CEO37856.1}. 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; CCAR020000003; CEO37856.1; -; Genomic_DNA. DR RefSeq; WP_036789335.1; NZ_LN794352.1. DR STRING; 1454202.PPBDW_80210___1; -. DR EnsemblBacteria; CEO37856; CEO37856; PPBDW_I10207. DR UniPathway; UPA00241; UER00353. DR Proteomes; UP000019762; 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 Decarboxylase {ECO:0000256|RuleBase:RU364078}; KW Flavoprotein {ECO:0000256|RuleBase:RU364078}; KW FMN {ECO:0000256|RuleBase:RU364078}; KW Ligase {ECO:0000256|RuleBase:RU364078, ECO:0000313|EMBL:CEO37856.1}; KW Lyase {ECO:0000256|RuleBase:RU364078, ECO:0000313|EMBL:CEO37856.1}. FT DOMAIN 7..179 FT /note="Flavoprotein" FT /evidence="ECO:0000259|Pfam:PF02441" FT DOMAIN 187..370 FT /note="DFP" FT /evidence="ECO:0000259|Pfam:PF04127" SQ SEQUENCE 404 AA; 42935 MW; A95EDE1A1DAEF4FC CRC64; MQTLAGKKIL LGISGGIAAY KCAELTRRLI ERGAQVQVVM TTAAQEFITP LTMQAVSGNP VSSSLLDPSA EASMGHIELA KWADLVLLAP ATADLIARIS AGMGNDLLTT LCLATNAPIA VAPAMNQQMY RNIATQENLA TLQRRGFTLW GPASGEQACG DVGPGRMLEP MQLVHHCEDF FQTPDLSNLN IMVTAGPTRE AIDPVRYLSN YSSGKMGFAI AAAAAKRGAK VTLISGPVNL ATPAGVTRID INSAIEMQQA ALTHAVKNQI FIACAAVADF RPAQIAAQKM KKQPGNEEMA IQLVKNPDIV ANVAALTNKR PFTVGFAAET QNVEHYARGK LAAKNLDLIC ANDVSVQGQG FNSDTNALHL YWPNGDKALP LTTKADLGQQ LVTEIVALYQ HATH //