ID   A0A7T4URB7_9GAMM        Unreviewed;       401 AA.
AC   A0A7T4URB7;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   24-JAN-2024, entry version 10.
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:QQD18200.1};
GN   ORFNames=I6N98_17980 {ECO:0000313|EMBL:QQD18200.1};
OS   Spongiibacter nanhainus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae; Spongiibacter.
OX   NCBI_TaxID=2794344 {ECO:0000313|EMBL:QQD18200.1, ECO:0000313|Proteomes:UP000596063};
RN   [1] {ECO:0000313|EMBL:QQD18200.1, ECO:0000313|Proteomes:UP000596063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=csc3.9 {ECO:0000313|Proteomes:UP000596063};
RA   Shan Y.;
RL   Submitted (DEC-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}.
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DR   EMBL; CP066167; QQD18200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7T4URB7; -.
DR   KEGG; snan:I6N98_17980; -.
DR   UniPathway; UPA00241; UER00353.
DR   Proteomes; UP000596063; 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; 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:UP000596063}.
FT   DOMAIN          8..180
FT                   /note="Flavoprotein"
FT                   /evidence="ECO:0000259|Pfam:PF02441"
FT   DOMAIN          187..366
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..401
FT                   /note="Phosphopantothenate--cysteine ligase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   ACT_SITE        159
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         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   401 AA;  42933 MW;  ECFAF426445B4AC1 CRC64;
     MKQLSNRHIL LGITGGIAAY KSAELVRRLQ DRGAEVKVVM TAAAMEFITP LTLQALSGNP
     VHTTLLDPEA EAGMGHIELA RWADVILVAP ASADFIARLA SGRGDDLLTT LCLATPAPIA
     LAPAMNQGMW RDPATQANLD TLRQRGIALF GPAAGEQACG DIGPGRMLEV DEIAELTADL
     FPNRALDGIK LRITAGPTRE AIDPVRYISN HSSGKMGFAL AAAAADAGAQ VTLISGPVNL
     ATPERVSRID VSSAQDMYDA SLADLQDCDI FIACAAVADY RPSEAVTQKI KKSADTLTLT
     LVRNPDIVSS VANSPQRPFT VGFAAETQDV LHYARDKLQR KKLDMIIAND VANTDIGFNS
     DDNRVVALWN GGEHAFDTMS KAQLSRRLIA LIAEHFRTER D
//