ID   A0A2Z5JVZ3_9ACTN        Unreviewed;       423 AA.
AC   A0A2Z5JVZ3;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   12-AUG-2020, entry version 6.
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=coaBC {ECO:0000313|EMBL:AXE84537.1};
GN   ORFNames=C1703_05955 {ECO:0000313|EMBL:AXE84537.1};
OS   Streptomyces sp. Go-475.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=2072505 {ECO:0000313|EMBL:AXE84537.1, ECO:0000313|Proteomes:UP000253251};
RN   [1] {ECO:0000313|EMBL:AXE84537.1, ECO:0000313|Proteomes:UP000253251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Go-475 {ECO:0000313|EMBL:AXE84537.1,
RC   ECO:0000313|Proteomes:UP000253251};
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 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}.
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DR   EMBL; CP026121; AXE84537.1; -; Genomic_DNA.
DR   UniPathway; UPA00241; UER00353.
DR   Proteomes; UP000253251; Chromosome.
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|ARBA:ARBA00022793,
KW   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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU364078}.
FT   DOMAIN          28..197
FT                   /note="Flavoprotein"
FT                   /evidence="ECO:0000259|Pfam:PF02441"
FT   DOMAIN          208..392
FT                   /note="DFP"
FT                   /evidence="ECO:0000259|Pfam:PF04127"
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
//