ID   C6AB60_BARGA            Unreviewed;       473 AA.
AC   C6AB60;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=dfp {ECO:0000313|EMBL:ACS50427.1};
GN   Synonyms=coaBC {ECO:0000256|HAMAP-Rule:MF_02225};
GN   OrderedLocusNames=Bgr_00350 {ECO:0000313|EMBL:ACS50427.1};
OS   Bartonella grahamii (strain as4aup).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=634504 {ECO:0000313|EMBL:ACS50427.1, ECO:0000313|Proteomes:UP000001489};
RN   [1] {ECO:0000313|EMBL:ACS50427.1, ECO:0000313|Proteomes:UP000001489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=as4aup {ECO:0000313|Proteomes:UP000001489};
RX   PubMed=19578403; DOI=10.1371/journal.pgen.1000546;
RA   Berglund E.C., Frank A.C., Calteau A., Vinnere Pettersson O., Granberg F.,
RA   Eriksson A.-S., Naeslund K., Holmberg M., Lindroos H., Andersson S.G.;
RT   "Run-off replication of host-adaptability genes is associated with gene
RT   transfer agents in the genome of mouse-infecting Bartonella grahamii.";
RL   PLoS Genet. 5:E1000546-E1000546(2009).
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; Evidence={ECO:0000256|HAMAP-
CC         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; Evidence={ECO:0000256|HAMAP-
CC         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; CP001562; ACS50427.1; -; Genomic_DNA.
DR   RefSeq; WP_012754466.1; NC_012846.1.
DR   AlphaFoldDB; C6AB60; -.
DR   STRING; 634504.Bgr_00350; -.
DR   KEGG; bgr:Bgr_00350; -.
DR   eggNOG; COG0452; Bacteria.
DR   HOGENOM; CLU_033319_0_1_5; -.
DR   OrthoDB; 9802554at2; -.
DR   UniPathway; UPA00241; UER00353.
DR   Proteomes; UP000001489; 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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 3.40.50.10300; CoaB-like; 1.
DR   Gene3D; 3.40.50.1950; Flavin prenyltransferase-like; 1.
DR   Gene3D; 1.10.1220.10; Met repressor-like; 1.
DR   HAMAP; MF_02225; CoaBC; 1.
DR   InterPro; IPR013321; Arc_rbn_hlx_hlx.
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   InterPro; IPR010985; Ribbon_hlx_hlx.
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.
DR   SUPFAM; SSF47598; Ribbon-helix-helix; 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}.
FT   DOMAIN          61..233
FT                   /note="Flavoprotein"
FT                   /evidence="ECO:0000259|Pfam:PF02441"
FT   DOMAIN          243..429
FT                   /note="DNA/pantothenate metabolism flavoprotein C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04127"
FT   REGION          1..246
FT                   /note="Phosphopantothenoylcysteine decarboxylase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   REGION          247..473
FT                   /note="Phosphopantothenate--cysteine ligase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         334
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         344
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         362..365
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         381
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         395
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         399
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
SQ   SEQUENCE   473 AA;  51276 MW;  8DE803197F2805C4 CRC64;
     MASITIRNLS PETKEALRIR AAQNGISMEE EVRRLLSNPT PFTTQPSHTS AVEVQSLKSK
     SLLLIIGGSI ASYKALDLIR RLQERGAHLK VVMTKAAQKF ITPLAAEALS GGTVYTDLFS
     REEEHDIGHI RLARNADLII LAPATANRIA KIANGIGDDL ADCILLAARC PLLIAPAMNP
     SMWAHSATIR NVAQLRADGV HIIGPEIGNM AERDEIGYGR MSEPLTIVAT IEALLNVHEK
     PLSDRHFIVT SGPTHEPIDP VRYLANRSSG KQGHAIATAL AHLGAKVTLI CGPVNLADPQ
     EVKTIHVETA QQMLQAVQTA LPADGAIFVA AVCDWRSQTQ SLHKIKKNAH KIPPSLHMVE
     NPDILATIGH APNRPSLVIG FAAETCDIIA NAQKKCVEKG ADFILANDIS LQLDGTSVMG
     ADTNQVYLVS KEKVEQWPHM SKQHVAQKLA NMIVSFFAPQ TPTPHEENIP HFK
//