COABC_VIBCH
ID COABC_VIBCH Reviewed; 399 AA.
AC Q9KVD1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=VC_0215;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF93391.1; -; Genomic_DNA.
DR PIR; A82351; A82351.
DR RefSeq; NP_229872.1; NC_002505.1.
DR RefSeq; WP_001190972.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KVD1; -.
DR SMR; Q9KVD1; -.
DR STRING; 243277.VC_0215; -.
DR DNASU; 2614569; -.
DR EnsemblBacteria; AAF93391; AAF93391; VC_0215.
DR GeneID; 57738952; -.
DR GeneID; 66941161; -.
DR KEGG; vch:VC_0215; -.
DR PATRIC; fig|243277.26.peg.197; -.
DR eggNOG; COG0452; Bacteria.
DR HOGENOM; CLU_033319_0_1_6; -.
DR OMA; LDMIVAN; -.
DR BioCyc; VCHO:VC0215-MON; -.
DR UniPathway; UPA00241; UER00353.
DR UniPathway; UPA00241; UER00354.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0071513; C:phosphopantothenoylcysteine decarboxylase complex; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
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..399
FT /note="Coenzyme A biosynthesis bifunctional protein CoaBC"
FT /id="PRO_0000182024"
FT REGION 1..190
FT /note="Phosphopantothenoylcysteine decarboxylase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT REGION 191..399
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 279
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
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 307..310
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT BINDING 326
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT BINDING 340
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
FT BINDING 344
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02225"
SQ SEQUENCE 399 AA; 42645 MW; 65192A744F857028 CRC64;
MQSLAGKKIL LGISGGIAAY KCAELTRRLV ERGATVQVVM THAAKEFITP LTMQAVSGRP
VSDSLLDPAA EASMGHIELA KWADLVLLAP ATADLIARMA AGMGNDLLTT LILATSAPVA
IAPAMNQQMY RNIATQENLQ TLIRRGYLTW GPAAGEQACG DVGPGRMLEP MELVAHCENF
FAPKILVGKR VLITAGPTRE ALDPVRYITN HSSGKMGFAL AKAAAQLGAD VTLVSGPVHL
PTPVGVNRID VQSGLEMHSA VMKEATSHQI FIACAAVADY RPQTVAEQKI KKSRDNDTLT
IEMVKNPDIV ASVAALTENR PFTVGFAAET QDVETYARSK LVRKNLDMIC ANDVSIAGQG
FNSNDNALTL FWKEGQHSLP LTSKDALASA VMHLIHEQM
