ID A0A2T6CNK4_9BACT Unreviewed; 400 AA.
AC A0A2T6CNK4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Coenzyme A biosynthesis bifunctional protein CoaBC {ECO:0000256|RuleBase:RU364078};
DE EC=4.1.1.36 {ECO:0000256|RuleBase:RU364078};
DE EC=6.3.2.5 {ECO:0000256|RuleBase:RU364078};
DE AltName: Full=DNA/pantothenate metabolism flavoprotein {ECO:0000256|RuleBase:RU364078};
GN Name=coaBC {ECO:0000313|EMBL:PTX91767.1};
GN ORFNames=DB354_18075 {ECO:0000313|EMBL:PTX91767.1};
OS Opitutus sp. ER46.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX NCBI_TaxID=2161864 {ECO:0000313|EMBL:PTX91767.1, ECO:0000313|Proteomes:UP000244023};
RN [1] {ECO:0000313|EMBL:PTX91767.1, ECO:0000313|Proteomes:UP000244023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ER46 {ECO:0000313|EMBL:PTX91767.1,
RC ECO:0000313|Proteomes:UP000244023};
RA Buenger W., Mueller J., Hurek T., Reinhold-Hurek B.;
RT "Genomic and phenotypic characterization of four novel plant-associated
RT Verrucomicrobia indicate a new subdivision with one cultivated member.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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|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|RuleBase:RU364078};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|RuleBase:RU364078};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 2/5. {ECO:0000256|RuleBase:RU364078}.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 3/5. {ECO:0000256|RuleBase:RU364078}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PPC synthetase
CC family. {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|RuleBase:RU364078}.
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:PTX91767.1}.
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DR EMBL; QAYX01000024; PTX91767.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6CNK4; -.
DR InParanoid; A0A2T6CNK4; -.
DR OrthoDB; 9802554at2; -.
DR UniPathway; UPA00241; UER00353.
DR Proteomes; UP000244023; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway.
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 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,
KW ECO:0000256|RuleBase:RU364078};
KW Flavoprotein {ECO:0000256|RuleBase:RU364078};
KW FMN {ECO:0000256|RuleBase:RU364078};
KW Ligase {ECO:0000256|RuleBase:RU364078, ECO:0000313|EMBL:PTX91767.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU364078};
KW Reference proteome {ECO:0000313|Proteomes:UP000244023}.
FT DOMAIN 3..174
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT DOMAIN 183..364
FT /note="DNA/pantothenate metabolism flavoprotein C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04127"
SQ SEQUENCE 400 AA; 42729 MW; 1A801D200B87B20B CRC64;
MSNVLFILTG SIACYKACEV ISQLVQRGHH VRPVASAAAL RFVGATTLEA LTHEKVRTDL
WAEGEALDHI NLDRWADVTV VCPATANTLN ALAAGLADNL VGSLLLAHDP HKPLLVAPAM
NPAMWKHPAT VAASRRLRSW GVQFIEPAAG RTACGEVGEG RLAEPETIVA AIDAALVRPE
HRLRVLVTSG GTSEPIDGVR VLTNISTGAT GAGIAEHFSR LGHDVLLVRA ATSVPLSAPG
REETYGSFGD LDAVLERRLR EEHFDVVIHA AAVSDYAIEA IEVDGQTWRP GAGKIPSQAT
PLIRLRRNPK LLDKLRSCSL NPAIRVVAFK LTKEADDAAM RAAVEAILAH GTADYVVQND
LAQREPDGAF PADIWGPQRT IVAHCRDRAD IALALATLLS
//
