ID A0A0X8FKK1_9LACT Unreviewed; 399 AA.
AC A0A0X8FKK1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=AWM75_02945 {ECO:0000313|EMBL:AMB99017.1}, SAMN04487985_1249
GN {ECO:0000313|EMBL:SDM56522.1};
OS Aerococcus urinaehominis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus.
OX NCBI_TaxID=128944 {ECO:0000313|EMBL:AMB99017.1, ECO:0000313|Proteomes:UP000062260};
RN [1] {ECO:0000313|EMBL:AMB99017.1, ECO:0000313|Proteomes:UP000062260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG42038B {ECO:0000313|EMBL:AMB99017.1,
RC ECO:0000313|Proteomes:UP000062260};
RX PubMed=27103727;
RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA Christensen J.J.;
RT "Complete Genome Sequences of Aerococcus christensenii CCUG 28831T,
RT Aerococcus sanguinicola CCUG 43001T, Aerococcus urinae CCUG 36881T,
RT Aerococcus urinaeequi CCUG 28094T, Aerococcus urinaehominis CCUG 42038 BT,
RT and Aerococcus viridans CCUG 4311T.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000062260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG42038B {ECO:0000313|Proteomes:UP000062260};
RA Carkaci D., Dargis R., Nielsen X.C., Skovgaard O., Fuursted K.,
RA Christensen J.J.;
RT "Six Aerococcus type strain genome sequencing and assembly using PacBio and
RT Illumina Hiseq.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SDM56522.1, ECO:0000313|Proteomes:UP000183325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15634 {ECO:0000313|EMBL:SDM56522.1,
RC ECO:0000313|Proteomes:UP000183325};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; CP014163; AMB99017.1; -; Genomic_DNA.
DR EMBL; FNHJ01000024; SDM56522.1; -; Genomic_DNA.
DR RefSeq; WP_067978027.1; NZ_FNHJ01000024.1.
DR AlphaFoldDB; A0A0X8FKK1; -.
DR STRING; 128944.AWM75_02945; -.
DR KEGG; auh:AWM75_02945; -.
DR OrthoDB; 9802554at2; -.
DR UniPathway; UPA00241; UER00353.
DR Proteomes; UP000062260; Chromosome.
DR Proteomes; UP000183325; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000062260}.
FT DOMAIN 5..174
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT DOMAIN 189..374
FT /note="DNA/pantothenate metabolism flavoprotein C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04127"
FT REGION 1..193
FT /note="Phosphopantothenoylcysteine decarboxylase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT REGION 194..399
FT /note="Phosphopantothenate--cysteine ligase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 282
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 292
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 313..316
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 329
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 343
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 347
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
SQ SEQUENCE 399 AA; 42962 MW; 38DF344685729062 CRC64;
MLNGKKIILA ITGGVAAYKI PNFARQLIKA GAEVRVVMTQ AACQFTTPFT LATLTKYPVL
LDQADYPDPV GHVHLADWAD LLLVVPATAN SLAKFAHGLA DNELTATWLA FNKTKIVVPA
MNEKMWQNPR TQANIKQLQA DGVQVIQPAY GFLAEGYQGQ GRMPETDQIL AAVQAQVAIN
EAGVPVDALS GQRVIISAGG TQEPLDPVRY LSNRSSGKMG LAIAHVASLL GAEVTLVRTP
SAKDLPVLPQ ITCLDVQNAR QLYQTMMTAE ADIVVMAAAV SDYRAKNPAD HKMKKTDDQR
ASGEMTIELV ENPDILASLD KTDRYTIGFA AETQNVLDYG RAKLVKKGAD MIVANDVSQA
GIGFGADDNA AYLITETGQV KIDQQSKYGL AAQIFKHMK
//
