ID L0IWZ2_9MYCO Unreviewed; 417 AA.
AC L0IWZ2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=Mycsm_02826 {ECO:0000313|EMBL:AGB23153.1};
OS Mycobacterium sp. JS623.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB23153.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) 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}.
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DR EMBL; CP003078; AGB23153.1; -; Genomic_DNA.
DR RefSeq; WP_015306732.1; NC_019966.1.
DR AlphaFoldDB; L0IWZ2; -.
DR STRING; 212767.Mycsm_02826; -.
DR KEGG; msa:Mycsm_02826; -.
DR PATRIC; fig|710686.3.peg.2850; -.
DR HOGENOM; CLU_033319_0_3_11; -.
DR OrthoDB; 9802554at2; -.
DR UniPathway; UPA00241; UER00353.
DR Proteomes; UP000010844; 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}.
FT DOMAIN 5..169
FT /note="Flavoprotein"
FT /evidence="ECO:0000259|Pfam:PF02441"
FT DOMAIN 187..382
FT /note="DNA/pantothenate metabolism flavoprotein C-terminal"
FT /evidence="ECO:0000259|Pfam:PF04127"
FT REGION 1..191
FT /note="Phosphopantothenoylcysteine decarboxylase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT REGION 192..417
FT /note="Phosphopantothenate--cysteine ligase"
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 335
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 353
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
FT BINDING 357
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225"
SQ SEQUENCE 417 AA; 43407 MW; 85DA64C511ED00CC CRC64;
MTERKRIIVG VAGGIAAYKA ATVVRQLTEA GHSVRVVPTE SALRFIGAAT FEALSGNPVH
TGVFDDVHEV PHVRIGQEAD LVVVAPATAD LLARAVAGRA DDLLTATLLT ARCPVMFAPA
MHTEMWFHPA TIENVTTLRR RGAIVLEPAS GRLTGADTGA GRLPEAEEIT TLAGLLLERG
DALPFDMAGV KVLVSAGGTR ETIDPVRFIG NRSSGKQGYA MARVMAQRGA DVTLIAGNTA
GLIDPAGVDV VHIGSAAQLK DAVSKHAPDA HVLVMAAAVA DFRPTNVQTS KIKKSADPNA
AAPVIELTRT DDVLAGAVRA RADGQLPNMR AIVGFAAETG DANGDVLFHA RAKLARKGCD
LLVVNAVGEN RAFEVDNNDG WLLASDGTES ALEHGSKTLM ASRIVDAIVA FLHSSGG
//
