ID   A0A2Z5JVZ3_9ACTN        Unreviewed;       423 AA.
AC   A0A2Z5JVZ3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   28-JUN-2023, entry version 18.
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:AXE84537.1};
GN   ORFNames=C1703_05955 {ECO:0000313|EMBL:AXE84537.1};
OS   Streptomyces sp. Go-475.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2072505 {ECO:0000313|EMBL:AXE84537.1, ECO:0000313|Proteomes:UP000253251};
RN   [1] {ECO:0000313|EMBL:AXE84537.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Go-475 {ECO:0000313|EMBL:AXE84537.1};
RX   PubMed=29946312; DOI=10.3389/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 Spectrometry.";
RL   Front. Microbiol. 9:1270-1270(2018).
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}.
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DR   EMBL; CP026121; AXE84537.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z5JVZ3; -.
DR   EnsemblBacteria; AXE84537; AXE84537; C1703_05955.
DR   UniPathway; UPA00241; UER00353.
DR   Proteomes; UP000253251; Chromosome.
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:UP000253251}.
FT   DOMAIN          28..197
FT                   /note="Flavoprotein"
FT                   /evidence="ECO:0000259|Pfam:PF02441"
FT   DOMAIN          208..392
FT                   /note="DNA/pantothenate metabolism flavoprotein C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04127"
FT   REGION          1..212
FT                   /note="Phosphopantothenoylcysteine decarboxylase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   REGION          213..423
FT                   /note="Phosphopantothenate--cysteine ligase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         301
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         311
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         329..332
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         349
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         363
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         367
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
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
//