ID A0A3T1CFP7_9SPHN Unreviewed; 583 AA.
AC A0A3T1CFP7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 20.
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=EKJ_06610 {ECO:0000313|EMBL:BBI19814.1};
OS Qipengyuania flava.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Sphingomonadales; Erythrobacteraceae; Qipengyuania.
OX NCBI_TaxID=192812 {ECO:0000313|EMBL:BBI19814.1, ECO:0000313|Proteomes:UP000290057};
RN [1] {ECO:0000313|EMBL:BBI19814.1, ECO:0000313|Proteomes:UP000290057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KJ5 {ECO:0000313|EMBL:BBI19814.1,
RC ECO:0000313|Proteomes:UP000290057};
RA Kanesaki Y., Brotosudarmo T., Moriuchi R., Awai K.;
RT "Complete genome sequence of Erythrobacter flavus KJ5.";
RL Submitted (JAN-2019) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-4'-phosphopantothenate + L-cysteine + CTP = N-[(R)-4-
CC phosphopantothenoyl]-L-cysteine + CMP + diphosphate + H(+);
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=N-[(R)-4-phosphopantothenoyl]-L-cysteine + H(+) = (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 -!- 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 -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 3/5. {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}.
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DR EMBL; AP019389; BBI19814.1; -; Genomic_DNA.
DR RefSeq; WP_172603216.1; NZ_AP019389.1.
DR AlphaFoldDB; A0A3T1CFP7; -.
DR UniPathway; UPA00241; UER00353.
DR Proteomes; UP000290057; Chromosome.
DR GO; GO:0071513; C:phosphopantothenoylcysteine decarboxylase complex; IEA:TreeGrafter.
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.
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 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:UP000290057}.
FT DOMAIN 25..197
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT DOMAIN 362..571
FT /note="DNA/pantothenate metabolism flavoprotein C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04127"
FT REGION 1..366
FT /note="Phosphopantothenoylcysteine decarboxylase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT REGION 219..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..583
FT /note="Phosphopantothenate--cysteine ligase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT COMPBIAS 229..248
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..294
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 454
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 464
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 481..484
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 500
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 514
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 518
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
SQ SEQUENCE 583 AA; 61086 MW; A01F5C0850646DFE CRC64;
MHLPIRAGAR GAEIAGRKRS VSGPKILLVI GGGIAAYKSC ELVRLIRKAG GEVTCVLTDG
GQQFVTPMAL AALSENKVYT SLFDLKDEVE MGHIQLSREA DLVVVCPATA DLLAKMAAGI
ADDLATTLIL ATDKPVLTVP AMNVRMWEHS ATQRNADWLR QAGVAVMDPD EGPMACGEFG
AGRMPEPPSI LARIAQELDL DLDLPELAAP APAQLAAPLA GDMSSDEGPL SEDWAEEPEM
GEEAEDEAPS NGGLGGLLSM IIPRTTETRT HDEIEAELEA LPEAEEEAAA EEPLDLPAPD
PAAGPILATK GKAAAAPPTD PSALAYDHGA GLQSVQTQSV TFENSPLAGQ GAFDPDPEHR
PLYGKHVLIT AGPTREPIDP VRYIANRSSG KQGFAIAAMA AAAGARVTLI AGPVHLPTPV
GVDRIDVETA EDMAEEVRRA LPVDIAFMVA AVADWKSRHV AGEKMKKRGS APPALILAEN
PDILASTAAG RKRPTLLIGF AAETENVVEN AKSKRKRKGA DWIVANNVAG DVGESVMGGD
LNQVHIVTAG GVESLPEMAK EDVARELVLR AAEALAPVEE SDD
//
