ID A0A2W5FM22_9BACT Unreviewed; 414 AA. AC A0A2W5FM22; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 24-JAN-2024, entry version 21. 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 ECO:0000313|EMBL:PZP55404.1}; GN ORFNames=DI586_06985 {ECO:0000313|EMBL:PZP55404.1}; OS Micavibrio aeruginosavorus. OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales; OC Pseudobdellovibrionaceae; Micavibrio. OX NCBI_TaxID=349221 {ECO:0000313|EMBL:PZP55404.1, ECO:0000313|Proteomes:UP000249739}; RN [1] {ECO:0000313|EMBL:PZP55404.1, ECO:0000313|Proteomes:UP000249739} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S2_006_000_R2_64 {ECO:0000313|EMBL:PZP55404.1}; RA Brooks B., Olm M.R., Firek B.A., Baker R., Thomas B.C., Morowitz M.J., RA Banfield J.F.; RT "Infants hospitalized years apart are colonized by the same room-sourced RT microbial strains."; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. 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 = (R)-4'- CC phosphopantetheine + CO2; 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 -!- 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:PZP55404.1}. 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; QFOT01000071; PZP55404.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2W5FM22; -. DR UniPathway; UPA00241; UER00353. DR Proteomes; UP000249739; Unassembled WGS sequence. 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; CoaB-like; 1. DR Gene3D; 3.40.50.1950; Flavin prenyltransferase-like; 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 NCBIfam; TIGR00521; coaBC_dfp; 1. DR PANTHER; PTHR14359; HOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY; 1. DR PANTHER; PTHR14359:SF6; PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE; 1. DR Pfam; PF04127; DFP; 1. DR Pfam; PF02441; Flavoprotein; 1. DR SUPFAM; SSF102645; CoaB-like; 1. DR SUPFAM; SSF52507; Homo-oligomeric flavin-containing Cys decarboxylases, HFCD; 1. PE 3: Inferred from homology; KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP- KW Rule:MF_02225}; 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 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 6..177 FT /note="Flavoprotein" FT /evidence="ECO:0000259|Pfam:PF02441" FT DOMAIN 185..370 FT /note="DNA/pantothenate metabolism flavoprotein C-terminal" FT /evidence="ECO:0000259|Pfam:PF04127" FT REGION 1..189 FT /note="Phosphopantothenoylcysteine decarboxylase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT REGION 190..414 FT /note="Phosphopantothenate--cysteine ligase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT ACT_SITE 158 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 277 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 287 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 305..308 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 324 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 338 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 342 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" SQ SEQUENCE 414 AA; 44667 MW; 5B7B6168C923DC80 CRC64; MDLQGKNILL VISGGIAAYK SLELIRLLRK AGANIVTILT SGGAHFVTPL SISALSENPV YMDLFSLKDE AEMGHIRLSR EADLIVVAPA SANTIAKLAQ GFAEDLASTA LLAANKKILM APAMNHMMWN NEATQENIRI LEQRGIDFIG PVEGEMACKE FGMGRMVEPE TILAAIKNYF SVKPLTGLKA LVTAGPTYEP IDPVRFIGNR SSGKQGYAIA QALTAQGADV TLISGPTNLK PPKNVSFIQI ETADQMHEQA MTSLPADIAI CAAAVADWKL ENPSDHKMKK RGGGEAPTIT LTENPDILKS ISIHKNRPGL VIGFAAETEE ILENAVKKLK SKGCDWIVAN QVGEKSNPVF GTDENEVILV SSANHEVWPR ISKQEVASRL VQKIISHVKD KTSDQLSRKT NAAN //