ID A0A7I9VSV2_9DELT Unreviewed; 406 AA. AC A0A7I9VSV2; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 03-MAY-2023, entry version 8. 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=AMYX_40390 {ECO:0000313|EMBL:GEJ59298.1}; OS Anaeromyxobacter diazotrophicus. OC Bacteria; Pseudomonadota; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=2590199 {ECO:0000313|EMBL:GEJ59298.1, ECO:0000313|Proteomes:UP000503640}; RN [1] {ECO:0000313|Proteomes:UP000503640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R267 {ECO:0000313|Proteomes:UP000503640}; RA Masuda Y., Yamanaka H., Xu Z.X., Shiratori Y., Aono T., Amachi S., RA Senoo K., Itoh H.; RT "Diazotrophic Anaeromyxobacter Isolates from Soils."; RL Appl. Environ. Microbiol. 86:e00956-e00920(2020). 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:GEJ59298.1}. 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; BJTG01000012; GEJ59298.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7I9VSV2; -. DR UniPathway; UPA00241; UER00353. DR Proteomes; UP000503640; 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 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. DR TIGRFAMs; TIGR00521; coaBC_dfp; 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000503640}. FT DOMAIN 8..178 FT /note="Flavoprotein" FT /evidence="ECO:0000259|Pfam:PF02441" FT DOMAIN 186..372 FT /note="DNA/pantothenate metabolism flavoprotein C-terminal" FT /evidence="ECO:0000259|Pfam:PF04127" FT REGION 1..190 FT /note="Phosphopantothenoylcysteine decarboxylase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT REGION 191..406 FT /note="Phosphopantothenate--cysteine ligase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 279 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 289 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 327 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 341 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 345 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" SQ SEQUENCE 406 AA; 42417 MW; DF59A45F949AAD7A CRC64; MHDFSGRTVV LGVGGGIAAY KACELARLFV KGGAQVRVAM TPAATRFVGP LTFQALTGAP VLVDLLAPEA DRAYGHLALA RAADLLVVAP ATADLIARLR AGMADDAVTT TALACEAPCL LAPAMNTRMW QNPAVRENVA ALARRGWEVV GPAAGALADG DVGEGRLAEP GDIADAAARL LGSRDLSGRR VLVSAGPTRE PLDPVRFISN PSTGKMGFAV ARVAARRGAE VVLVTGPVDL PDPPGVRTIR VVTAEEMASA VEEEAREIDL YVGAAAVSDF KPRVAAATKK KKSDEDEEVT LTRTPDILAA LGKRFAGKAE APILVGFAAE TEALLQNARK KLAAKRCDLV VANKVGRPGV GFASDRNRVT LVGPGERANI EGTKEQVADA ILDWVVPVLE ERRPRG //