ID Q4JBG1_SULAC Unreviewed; 409 AA. AC Q4JBG1; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 02-DEC-2020, entry version 79. 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 OrderedLocusNames=Saci_0458 {ECO:0000313|EMBL:AAY79868.1}; OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC OS 15157 / NCIMB 11770). OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=330779 {ECO:0000313|EMBL:AAY79868.1, ECO:0000313|Proteomes:UP000001018}; RN [1] {ECO:0000313|EMBL:AAY79868.1, ECO:0000313|Proteomes:UP000001018} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770 RC {ECO:0000313|Proteomes:UP000001018}; RX PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005; RA Chen L., Brugger K., Skovgaard M., Redder P., She Q., Torarinsson E., RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.; RT "The genome of Sulfolobus acidocaldarius, a model organism of the RT Crenarchaeota."; RL J. Bacteriol. 187:4992-4999(2005). 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 -!- 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 -!- 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|HAMAP-Rule:MF_02225}; 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. CC {ECO:0000256|HAMAP-Rule:MF_02225}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PPC synthetase CC family. {ECO:0000256|HAMAP-Rule:MF_02225}. 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}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02225}. 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; CP000077; AAY79868.1; -; Genomic_DNA. DR RefSeq; WP_011277370.1; NC_007181.1. DR STRING; 330779.Saci_0458; -. DR EnsemblBacteria; AAY79868; AAY79868; Saci_0458. DR GeneID; 3474549; -. DR KEGG; sai:Saci_0458; -. DR PATRIC; fig|330779.12.peg.455; -. DR eggNOG; arCOG01704; Archaea. DR HOGENOM; CLU_033319_0_3_2; -. DR OMA; AMNVNMY; -. DR BioCyc; SACI330779:G1G4L-446-MONOMER; -. DR UniPathway; UPA00241; -. DR Proteomes; UP000001018; 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; -; 1. DR Gene3D; 3.40.50.1950; -; 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 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, ECO:0000256|HAMAP- KW Rule:MF_02225}; Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02225}; KW FMN {ECO:0000256|HAMAP-Rule:MF_02225}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_02225}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02225, KW ECO:0000313|EMBL:AAY79868.1}; 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:UP000001018}. FT DOMAIN 19..173 FT /note="Flavoprotein" FT /evidence="ECO:0000259|Pfam:PF02441" FT DOMAIN 191..377 FT /note="DFP" FT /evidence="ECO:0000259|Pfam:PF04127" FT REGION 1..195 FT /note="Phosphopantothenoylcysteine decarboxylase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT REGION 196..409 FT /note="Phosphopantothenate--cysteine ligase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 286 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 296 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 328 FT /note="CTP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 346 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" SQ SEQUENCE 409 AA; 45552 MW; E22624F282D48029 CRC64; MVHPSKKIIG EVSRELLNKK ILVGVTASVS IYKSLDLVRA LMRRGANVRV IMSKDSIRLI NPMMFHWATG EEPVVSVGGE IEHVELAEEY DALVIAPSTA NTISKLANGI ADTSITLTAL NFVGIKKPVI LVPAMHLTMY EAPQFKENIE KLVKQGIEII SPEITRDVAH YPDIEYLSSY ITSFLLRGKD LKGYKIVVTA GPTREYIDPV RFISNSSSGT MGVSIANEAY FRGADVILVH GPLSSSVKPY TKRIRVDTTQ EMAENVEKLV RDEKYGIVIL AGAPADFKPK NTASSKIDSH SEVPKVELET TPKISSKLSI YRPLLVGFSA ETVNSDEELI EKAKMKKERH KFDIIVANNV KRKDIGFSSE YNEVIVIGNS FVRKLEKNYK TIIARELLDI VKYEVSRKV //