ID A0A143ZWZ6_9FIRM Unreviewed; 402 AA.
AC A0A143ZWZ6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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:CZT58004.1};
GN ORFNames=BN3661_02275 {ECO:0000313|EMBL:CZT58004.1};
OS Eubacteriaceae bacterium CHKCI005.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae.
OX NCBI_TaxID=1780381 {ECO:0000313|EMBL:CZT58004.1, ECO:0000313|Proteomes:UP000199521};
RN [1] {ECO:0000313|EMBL:CZT58004.1, ECO:0000313|Proteomes:UP000199521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHKC5 {ECO:0000313|EMBL:CZT58004.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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 -!- 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; FJVJ01000046; CZT58004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143ZWZ6; -.
DR STRING; 1780381.BN3661_02275; -.
DR UniPathway; UPA00241; UER00353.
DR Proteomes; UP000199521; 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 NCBIfam; TIGR00521; coaBC_dfp; 1.
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};
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:UP000199521}.
FT DOMAIN 6..174
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT DOMAIN 187..369
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..402
FT /note="Phosphopantothenate--cysteine ligase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT ACT_SITE 158
FT /note="Proton donor"
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 324
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 338
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 342
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
SQ SEQUENCE 402 AA; 43725 MW; 324D06D975B8270D CRC64;
MLLSGKHILL GVCGGIAAYK AAALASLLTK QGAVVHPILT KNAMRFVSPI TFEGVSGQRC
FTDTFDRDTE FRVPHIKLAQ MADAVLVAPA SANTIAKLSH GLADDMLTST LLACRCKKLI
APAMNTAMFE NPVTQDNLKT LEHYGWTVIQ PAYGHLACGD TGAGKMPEPE YLLQYMLFYL
AEQKDMTGFN VLVTAGPTRE SLDPVRYLTN HSSGKMGYEL AVNAARRGAH VTLVTGSDQL
PDPPFVDIIH VESAQDMFDA VTAVSHQQDI LAFAAAVADY RPATVSQQKI KKTSDHSVLE
LTRTPDILQT VGLSKKPGQL ICGFSMETQD LLDHSQEKRK KKNADLMCAN SLREEGAGFG
VDTNIITLIS DQGVEKLPLL SKYDVSRKIW DAMLSMKSHS NS
//
