ID A0A099WCF6_9LIST Unreviewed; 400 AA.
AC A0A099WCF6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:MBC1228940.1};
GN ORFNames=EP57_08025 {ECO:0000313|EMBL:KGL41780.1}, HB810_02960
GN {ECO:0000313|EMBL:MBC1245543.1}, HB816_00555
GN {ECO:0000313|EMBL:MBC1228940.1}, HB836_15765
GN {ECO:0000313|EMBL:MBC1403050.1}, HB856_04065
GN {ECO:0000313|EMBL:MBC1357379.1}, HB900_02985
GN {ECO:0000313|EMBL:MBC1573408.1}, HB904_04965
GN {ECO:0000313|EMBL:MBC1615525.1}, HCA55_15995
GN {ECO:0000313|EMBL:MBC1798239.1}, HCA72_02920
GN {ECO:0000313|EMBL:MBC2046809.1}, HCA73_15415
GN {ECO:0000313|EMBL:MBC1914038.1}, HCA78_10730
GN {ECO:0000313|EMBL:MBC2004245.1}, HCB06_04225
GN {ECO:0000313|EMBL:MBC2115817.1}, HCB25_00140
GN {ECO:0000313|EMBL:MBC2242450.1}, HCB26_03320
GN {ECO:0000313|EMBL:MBC2165609.1}, HCB27_08825
GN {ECO:0000313|EMBL:MBC2176717.1}, HCC18_02060
GN {ECO:0000313|EMBL:MBC2315614.1}, HCI99_15840
GN {ECO:0000313|EMBL:MBC1493292.1}, HCJ32_05775
GN {ECO:0000313|EMBL:MBC1944471.1};
OS Listeria booriae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1552123 {ECO:0000313|EMBL:KGL41780.1, ECO:0000313|Proteomes:UP000029844};
RN [1] {ECO:0000313|EMBL:KGL41780.1, ECO:0000313|Proteomes:UP000029844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL A5-0281 {ECO:0000313|EMBL:KGL41780.1,
RC ECO:0000313|Proteomes:UP000029844};
RA den Bakker H.C.;
RT "Novel Listeriaceae from food processing environments.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000519573, ECO:0000313|Proteomes:UP000525521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL L7-0029 {ECO:0000313|EMBL:MBC2315614.1,
RC ECO:0000313|Proteomes:UP000576477}, FSL L7-0153
RC {ECO:0000313|EMBL:MBC2242450.1, ECO:0000313|Proteomes:UP000550367},
RC FSL L7-0245 {ECO:0000313|EMBL:MBC2165609.1,
RC ECO:0000313|Proteomes:UP000519573}, FSL L7-0259
RC {ECO:0000313|EMBL:MBC2176717.1, ECO:0000313|Proteomes:UP000541735},
RC FSL L7-0360 {ECO:0000313|EMBL:MBC2115817.1,
RC ECO:0000313|Proteomes:UP000529446}, FSL L7-0435
RC {ECO:0000313|EMBL:MBC2004245.1, ECO:0000313|Proteomes:UP000546806},
RC FSL L7-0514 {ECO:0000313|EMBL:MBC2046809.1,
RC ECO:0000313|Proteomes:UP000588249}, FSL L7-0729
RC {ECO:0000313|EMBL:MBC1944471.1, ECO:0000313|Proteomes:UP000552349},
RC FSL L7-0811 {ECO:0000313|EMBL:MBC1914038.1,
RC ECO:0000313|Proteomes:UP000574808}, FSL L7-0990
RC {ECO:0000313|EMBL:MBC1798239.1, ECO:0000313|Proteomes:UP000548082},
RC FSL L7-1299 {ECO:0000313|EMBL:MBC1615525.1,
RC ECO:0000313|Proteomes:UP000574104}, FSL L7-1385
RC {ECO:0000313|EMBL:MBC1573408.1, ECO:0000313|Proteomes:UP000571880},
RC FSL L7-1547 {ECO:0000313|EMBL:MBC1493292.1,
RC ECO:0000313|Proteomes:UP000533953}, FSL L7-1658
RC {ECO:0000313|EMBL:MBC1403050.1, ECO:0000313|Proteomes:UP000544413},
RC FSL L7-1698 {ECO:0000313|EMBL:MBC1357379.1,
RC ECO:0000313|Proteomes:UP000525521}, FSL L7-1827
RC {ECO:0000313|EMBL:MBC1245543.1, ECO:0000313|Proteomes:UP000574869},
RC and FSL L7-1831 {ECO:0000313|EMBL:MBC1228940.1,
RC ECO:0000313|Proteomes:UP000585770};
RA Liao J., Wiedmann M.;
RT "Soil Listeria distribution.";
RL Submitted (MAR-2020) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGL41780.1}.
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DR EMBL; JNFA01000019; KGL41780.1; -; Genomic_DNA.
DR EMBL; JAARON010000001; MBC1228940.1; -; Genomic_DNA.
DR EMBL; JAAROQ010000001; MBC1245543.1; -; Genomic_DNA.
DR EMBL; JAARPI010000001; MBC1357379.1; -; Genomic_DNA.
DR EMBL; JAARPT010000012; MBC1403050.1; -; Genomic_DNA.
DR EMBL; JAASTX010000030; MBC1493292.1; -; Genomic_DNA.
DR EMBL; JAARRX010000002; MBC1573408.1; -; Genomic_DNA.
DR EMBL; JAARSH010000003; MBC1615525.1; -; Genomic_DNA.
DR EMBL; JAARVD010000009; MBC1798239.1; -; Genomic_DNA.
DR EMBL; JAARWI010000010; MBC1914038.1; -; Genomic_DNA.
DR EMBL; JAASVH010000002; MBC1944471.1; -; Genomic_DNA.
DR EMBL; JAARWW010000004; MBC2004245.1; -; Genomic_DNA.
DR EMBL; JAARWT010000001; MBC2046809.1; -; Genomic_DNA.
DR EMBL; JAARXI010000002; MBC2115817.1; -; Genomic_DNA.
DR EMBL; JAARYH010000001; MBC2165609.1; -; Genomic_DNA.
DR EMBL; JAARYD010000004; MBC2176717.1; -; Genomic_DNA.
DR EMBL; JAARYY010000001; MBC2242450.1; -; Genomic_DNA.
DR EMBL; JAARZZ010000001; MBC2315614.1; -; Genomic_DNA.
DR STRING; 1552123.EP57_08025; -.
DR eggNOG; COG0452; Bacteria.
DR OrthoDB; 9802554at2; -.
DR UniPathway; UPA00241; UER00353.
DR Proteomes; UP000029844; Unassembled WGS sequence.
DR Proteomes; UP000519573; Unassembled WGS sequence.
DR Proteomes; UP000525521; Unassembled WGS sequence.
DR Proteomes; UP000529446; Unassembled WGS sequence.
DR Proteomes; UP000533953; Unassembled WGS sequence.
DR Proteomes; UP000541735; Unassembled WGS sequence.
DR Proteomes; UP000544413; Unassembled WGS sequence.
DR Proteomes; UP000546806; Unassembled WGS sequence.
DR Proteomes; UP000548082; Unassembled WGS sequence.
DR Proteomes; UP000550367; Unassembled WGS sequence.
DR Proteomes; UP000552349; Unassembled WGS sequence.
DR Proteomes; UP000571880; Unassembled WGS sequence.
DR Proteomes; UP000574104; Unassembled WGS sequence.
DR Proteomes; UP000574808; Unassembled WGS sequence.
DR Proteomes; UP000574869; Unassembled WGS sequence.
DR Proteomes; UP000576477; Unassembled WGS sequence.
DR Proteomes; UP000585770; Unassembled WGS sequence.
DR Proteomes; UP000588249; 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:UP000029844}.
FT DOMAIN 4..174
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT DOMAIN 185..367
FT /note="DNA/pantothenate metabolism flavoprotein C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04127"
FT REGION 1..189
FT /note="Phosphopantothenoylcysteine decarboxylase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT REGION 190..400
FT /note="Phosphopantothenate--cysteine ligase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT ACT_SITE 156
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 278
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 288
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 323
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 337
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 341
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
SQ SEQUENCE 400 AA; 43459 MW; A18585FF7F9112A3 CRC64;
MNGKNILLAV SGGIAVYKAV ALTSKLTQAG ANVKVMMTKS AQEFVPPLSF QVLSRNDVYT
DTFDEKDSGV VAHINLADWA DLVIVAPATA NVIGKMANGI ADDMVTTTLL ATEAPIWVAP
AMNVHMIAHP AVVRNINQLY ADGVRFIEPS EGYLACGYVG RGRLEEPERI VGHLTAYFTE
KNTTLAGRKV VITAGATIEK LDPVRYFTNH STGKMGFAVA ETAARYGAEV VLVTSSTKLP
VPHGVAVHYI ETAQEMYDEV MKHQDSADIF VMSAAVADYT PKVIHEHKIK KQPGDFAIEM
VRTKDILAEI GQNKRDTQVV IGFAAETQNV KENALKKLHS KNADMIVANN VAQIGAGFGV
DTNQVTFYGH DDAETVFPLL SKQEVAREII EQAARFLEEK
//
