ID   A0A926M6H3_9PROT        Unreviewed;       399 AA.
AC   A0A926M6H3;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   28-JUN-2023, entry version 3.
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:MBD1141769.1};
GN   ORFNames=IDH31_01295 {ECO:0000313|EMBL:MBD1141769.1};
OS   Pelagibacterales bacterium SAG-MED32.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Pelagibacterales.
OX   NCBI_TaxID=2760034 {ECO:0000313|EMBL:MBD1141769.1, ECO:0000313|Proteomes:UP000651905};
RN   [1] {ECO:0000313|EMBL:MBD1141769.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SAG-MED32 {ECO:0000313|EMBL:MBD1141769.1};
RX   PubMed=31840364;
RA   Haro-Moreno J.M., Rodriguez-Valera F., Rosselli R., Martinez-Hernandez F.,
RA   Roda-Garcia J.J., Gomez M.L., Fornas O., Martinez-Garcia M.,
RA   Lopez-Perez M.;
RT   "Ecogenomics of the SAR11 clade.";
RL   Environ. Microbiol. 22:1748-1763(2020).
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:MBD1141769.1}.
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; JACWEC010000005; MBD1141769.1; -; Genomic_DNA.
DR   Proteomes; UP000651905; 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   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.
DR   TIGRFAMs; TIGR00521; coaBC_dfp; 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:UP000651905}.
FT   DOMAIN          5..175
FT                   /note="Flavoprotein"
FT                   /evidence="ECO:0000259|Pfam:PF02441"
FT   DOMAIN          191..369
FT                   /note="DNA/pantothenate metabolism flavoprotein C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04127"
FT   REGION          1..191
FT                   /note="Phosphopantothenoylcysteine decarboxylase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   REGION          192..399
FT                   /note="Phosphopantothenate--cysteine ligase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   ACT_SITE        157
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         325
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         339
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         343
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
SQ   SEQUENCE   399 AA;  43960 MW;  2AFD8521889622CA CRC64;
     MNKSKKVLLI ITGGIAAYKS LEIIRGLKAN NIDVTCILTK SGSEFVTPLS IESLSENKVY
     TDLFNLTDEH EMGHIQLSRQ ADVILVAPAT ANIMSKIAYG NTDDLASTVL VATNKPIIVA
     PAMNVRMWLN NATQRNIQTL RNDGIKFVGP ENGEMACGEY GEGRMSEPSE IIKYTNDFIN
     SLDFKPLRDF SALVTSGPTK EMIDPVRFIS NESSGKQGFT IAEKLSSLGA YTTLISGPTK
     LPNPNVDKVV HVSSADEMML ECDKALPVNI AICAAAVADY KVMKQSETKI KKNGSRLDIT
     LEENPDILSR LSKRNDKRPG LVVGFAAETE KLEENSKIKL EKKGCDWILG NNVSNGQVIG
     KDTNEIHFIS KSETENWKQM RKEEVAEKLS HKIVQHLKS
//