COABC_ALIF1
ID COABC_ALIF1 Reviewed; 409 AA.
AC Q5E8M6;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Coenzyme A biosynthesis bifunctional protein CoaBC {ECO:0000255|HAMAP-Rule:MF_02225};
DE AltName: Full=DNA/pantothenate metabolism flavoprotein {ECO:0000255|HAMAP-Rule:MF_02225};
DE AltName: Full=Phosphopantothenoylcysteine synthetase/decarboxylase {ECO:0000255|HAMAP-Rule:MF_02225};
DE Short=PPCS-PPCDC {ECO:0000255|HAMAP-Rule:MF_02225};
DE Includes:
DE RecName: Full=Phosphopantothenoylcysteine decarboxylase {ECO:0000255|HAMAP-Rule:MF_02225};
DE Short=PPC decarboxylase {ECO:0000255|HAMAP-Rule:MF_02225};
DE Short=PPC-DC {ECO:0000255|HAMAP-Rule:MF_02225};
DE EC=4.1.1.36 {ECO:0000255|HAMAP-Rule:MF_02225};
DE AltName: Full=CoaC {ECO:0000255|HAMAP-Rule:MF_02225};
DE Includes:
DE RecName: Full=Phosphopantothenate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_02225};
DE EC=6.3.2.5 {ECO:0000255|HAMAP-Rule:MF_02225};
DE AltName: Full=CoaB {ECO:0000255|HAMAP-Rule:MF_02225};
DE AltName: Full=Phosphopantothenoylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_02225};
DE Short=PPC synthetase {ECO:0000255|HAMAP-Rule:MF_02225};
DE Short=PPC-S {ECO:0000255|HAMAP-Rule:MF_02225};
GN Name=coaBC {ECO:0000255|HAMAP-Rule:MF_02225}; OrderedLocusNames=VF_0125;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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:0000255|HAMAP-Rule:MF_02225}.
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:0000255|HAMAP-Rule:MF_02225};
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:0000255|HAMAP-Rule:MF_02225};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02225};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02225};
CC Note=Binds 1 FMN per subunit. {ECO:0000255|HAMAP-Rule:MF_02225};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 2/5. {ECO:0000255|HAMAP-Rule:MF_02225}.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 3/5. {ECO:0000255|HAMAP-Rule:MF_02225}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HFCD (homo-
CC oligomeric flavin containing Cys decarboxylase) superfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02225}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PPC synthetase
CC family. {ECO:0000255|HAMAP-Rule:MF_02225}.
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DR EMBL; CP000020; AAW84620.1; -; Genomic_DNA.
DR RefSeq; WP_011260987.1; NC_006840.2.
DR RefSeq; YP_203508.1; NC_006840.2.
DR AlphaFoldDB; Q5E8M6; -.
DR SMR; Q5E8M6; -.
DR STRING; 312309.VF_0125; -.
DR PRIDE; Q5E8M6; -.
DR EnsemblBacteria; AAW84620; AAW84620; VF_0125.
DR KEGG; vfi:VF_0125; -.
DR PATRIC; fig|312309.11.peg.124; -.
DR eggNOG; COG0452; Bacteria.
DR HOGENOM; CLU_033319_0_1_6; -.
DR OMA; LDMIVAN; -.
DR OrthoDB; 1346419at2; -.
DR UniPathway; UPA00241; UER00353.
DR UniPathway; UPA00241; UER00354.
DR Proteomes; UP000000537; Chromosome I.
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; -; 1.
DR Gene3D; 3.40.50.1950; -; 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 Pfam; PF04127; DFP; 1.
DR Pfam; PF02441; Flavoprotein; 1.
DR SUPFAM; SSF102645; SSF102645; 1.
DR SUPFAM; SSF52507; SSF52507; 1.
DR TIGRFAMs; TIGR00521; coaBC_dfp; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Flavoprotein; FMN; Ligase; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Reference proteome.
FT CHAIN 1..409
FT /note="Coenzyme A biosynthesis bifunctional protein CoaBC"
FT /id="PRO_0000182025"
FT REGION 1..200
FT /note="Phosphopantothenoylcysteine decarboxylase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT REGION 201..409
FT /note="Phosphopantothenate--cysteine ligase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT ACT_SITE 159
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT BINDING 289
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT BINDING 299
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT BINDING 317..320
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT BINDING 336
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT BINDING 350
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT BINDING 354
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
SQ SEQUENCE 409 AA; 43621 MW; 7B248F9CAC97B818 CRC64;
MASLAGKRIL LGISGGIAAY KCAELTRRLI ERGAEVRVVM TKAAKEFITP LTMQAVSGHP
VADSLLDPAA EASMGHIELA KWADIVLLAP ATADLIARMA AGMGNDLLST LVLATDSPVA
VSPAMNQQMY SNIATQENIA TLARRGMHIW GPAAGQQACG DVGMGRMLEP MELVHLCEDF
FQANSCEQAE ADEKPLKGQS LLITAGPTRE AIDPVRYISN HSSGKMGFAI AEAAAQLGAN
VTLVSGPVNL ATPENVKRID IESAEQMHGA VMKNAQSHSI FIACAAVADF KLSQVATQKL
KKTADEDGMT LHMVKNPDIV ASVAALTNQR PFTVGFAAET QDVEKYARGK LERKNLDMIC
ANDVSVQGQG FNSDNNALHL YWKEGDKALP LTTKSELGKA IMLEIVEKL
