ID D7CLQ1_SYNLT Unreviewed; 396 AA.
AC D7CLQ1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 OrderedLocusNames=Slip_0856 {ECO:0000313|EMBL:ADI01636.1};
OS Syntrophothermus lipocalidus (strain DSM 12680 / TGB-C1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophothermus.
OX NCBI_TaxID=643648 {ECO:0000313|EMBL:ADI01636.1, ECO:0000313|Proteomes:UP000000378};
RN [1] {ECO:0000313|Proteomes:UP000000378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378};
RX DOI=10.4056/sigs.1233249;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Djao O., Zhang X., Lucas S., Lapidus A., Glavina Del Rio T., Nolan M.,
RA Tice H., Cheng J., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.,
RA Jeffries C., Rohde M., Sikorski J., Spring S., Goker M., Detter J.,
RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA Klenk H.;
RT "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB-
RT C1T).";
RL Stand. Genomic Sci. 3:267-275(2010).
RN [2] {ECO:0000313|EMBL:ADI01636.1, ECO:0000313|Proteomes:UP000000378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378};
RX PubMed=21304731;
RA Djao O.D., Zhang X., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Rohde M., Sikorski J., Spring S., Goker M., Detter J.C.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB-
RT C1).";
RL Stand. Genomic Sci. 3:268-275(2010).
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 ---------------------------------------------------------------------------
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; CP002048; ADI01636.1; -; Genomic_DNA.
DR RefSeq; WP_013175038.1; NC_014220.1.
DR AlphaFoldDB; D7CLQ1; -.
DR STRING; 643648.Slip_0856; -.
DR KEGG; slp:Slip_0856; -.
DR eggNOG; COG0452; Bacteria.
DR HOGENOM; CLU_033319_0_1_9; -.
DR OrthoDB; 9802554at2; -.
DR UniPathway; UPA00241; UER00353.
DR Proteomes; UP000000378; 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:UP000000378}.
FT DOMAIN 5..178
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT DOMAIN 186..367
FT /note="DNA/pantothenate metabolism flavoprotein C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04127"
FT REGION 1..189
FT /note="Phosphopantothenoylcysteine decarboxylase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT REGION 190..396
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 278
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 288
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 304..307
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 322
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 336
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 340
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
SQ SEQUENCE 396 AA; 42954 MW; 7BE958385F0F24D4 CRC64;
MEFNKTVGIG VSGGIAAYKT ADLVSRLAKA GADVHVIMTR NATRFVTPLT FRTLSGNPVL
VDSFEENNRW KVQHIGVAEE IDVLVICPAT ANIIGKMAHG LADDLLSTVV LATRAPILVV
PAMNTNMYAN RIVQDNLQRL REYGFHVLEP EEGELACGAK GKGRLPDIEG IYHKIMSLLN
PRLDFAGKTV LVTSGPTREA IDPVRFISNR STGKMGHALA RAALARGAKV ILVSGPTDLP
VPLGVEYVPV TSAEEMYRRV RDYYRDCDVV IGAAAVADYR PRQFSQQKLK KGDSDLVIEL
TRNPDILAEL GKDKGNRILV GFAAETQDLI ANAVDKMHKK NLDLLVANDV TLEGAGFGTD
TNIVTIISRQ GDTTPLPGMA KSDLANVILD RISELF
//
