GenomeNet

Database: UniProt
Entry: A0A1Q6V149_9BACT
LinkDB: A0A1Q6V149_9BACT
Original site: A0A1Q6V149_9BACT 
ID   A0A1Q6V149_9BACT        Unreviewed;       400 AA.
AC   A0A1Q6V149;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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   ORFNames=BHW64_03315 {ECO:0000313|EMBL:OLA94532.1};
OS   Candidatus Melainabacteria bacterium LEY3_CP_29_8.
OC   Bacteria; Candidatus Melainabacteria.
OX   NCBI_TaxID=1913460 {ECO:0000313|EMBL:OLA94532.1, ECO:0000313|Proteomes:UP000233660};
RN   [1] {ECO:0000313|EMBL:OLA94532.1, ECO:0000313|Proteomes:UP000233660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LEY3_CP_29_8 {ECO:0000313|EMBL:OLA94532.1};
RX   PubMed=27819664; DOI=10.1038/nbt.3704;
RA   Brown C.T., Olm M.R., Thomas B.C., Banfield J.F.;
RT   "Measurement of bacterial replication rates in microbial communities.";
RL   Nat. Biotechnol. 34:1256-1263(2016).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLA94532.1}.
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; MNUB01000047; OLA94532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q6V149; -.
DR   UniPathway; UPA00241; UER00353.
DR   Proteomes; UP000233660; Unassembled WGS sequence.
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}.
FT   DOMAIN          10..180
FT                   /note="Flavoprotein"
FT                   /evidence="ECO:0000259|Pfam:PF02441"
FT   DOMAIN          190..371
FT                   /note="DNA/pantothenate metabolism flavoprotein C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04127"
FT   REGION          1..194
FT                   /note="Phosphopantothenoylcysteine decarboxylase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   REGION          195..400
FT                   /note="Phosphopantothenate--cysteine ligase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   ACT_SITE        161
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         281
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         291
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         307..310
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT   BINDING         326
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"
FT   BINDING         344
FT                   /ligand="CTP"
FT                   /ligand_id="ChEBI:CHEBI:37563"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
SQ   SEQUENCE   400 AA;  43965 MW;  D245F215D0219AB4 CRC64;
     MILHNDLTNK TILLGVTGGI AAYKVPNLIR MLKKKGANVV VVATSNALNF VTKLTLQTVS
     NNKVHVDEFD TKDFDIEHIA LSKKADLMLI APLSANTLGK IANGIADNLL TSIVLAFNKP
     IVLCPAMNTN MWQNAIVQDN LKKLKNSNFN IIKPISGMLA CGDIGVGKMP DENLIVENIV
     SILNYENKFL KGKNVLITAG GTSEPIDCVR FITNKSSGKM GLALAKQASY LGACVHLIST
     FEVNNPQFQV TKVQTALQMQ DVVFKNLQQA DIVIMAAAVS DFRCQNPSEQ KIKKNDGGLT
     LNLVKNPDIL TQIAKEKSEN QIIVGFCAES QNLIDNAKEK IKAKNSDFIV ANDISNKNIG
     FNSDNNEVFI VDKNLNVEKF EFDTKDKIAY EILNYVNKNY
//
DBGET integrated database retrieval system