ID A0A7T4URB7_9GAMM Unreviewed; 401 AA. AC A0A7T4URB7; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 19-JAN-2022, entry version 2. 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 ECO:0000313|EMBL:QQD18200.1}; GN ORFNames=I6N98_17980 {ECO:0000313|EMBL:QQD18200.1}; OS Spongiibacter sp. CSC3.9. OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales; OC Spongiibacteraceae; Spongiibacter; unclassified Spongiibacter. OX NCBI_TaxID=2794344 {ECO:0000313|EMBL:QQD18200.1, ECO:0000313|Proteomes:UP000596063}; RN [1] {ECO:0000313|EMBL:QQD18200.1, ECO:0000313|Proteomes:UP000596063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=csc3.9 {ECO:0000313|Proteomes:UP000596063}; RA Shan Y.; RL Submitted (DEC-2020) 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; CP066167; QQD18200.1; -; Genomic_DNA. DR UniPathway; UPA00241; UER00353. DR Proteomes; UP000596063; Chromosome. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.10300; -; 1. DR Gene3D; 3.40.50.1950; -; 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 Pfam; PF04127; DFP; 1. DR Pfam; PF02441; Flavoprotein; 1. DR SUPFAM; SSF102645; SSF102645; 1. DR SUPFAM; SSF52507; SSF52507; 1. DR TIGRFAMs; TIGR00521; coaBC_dfp; 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 8..179 FT /note="Flavoprotein" FT /evidence="ECO:0000259|Pfam:PF02441" FT DOMAIN 187..366 FT /note="DFP" FT /evidence="ECO:0000259|Pfam:PF04127" FT NP_BIND 305..308 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT REGION 1..190 FT /note="Phosphopantothenoylcysteine decarboxylase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT REGION 191..401 FT /note="Phosphopantothenate--cysteine ligase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT ACT_SITE 159 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 279 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 289 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 323 FT /note="CTP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 337 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" FT BINDING 341 FT /note="CTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02225" SQ SEQUENCE 401 AA; 42933 MW; ECFAF426445B4AC1 CRC64; MKQLSNRHIL LGITGGIAAY KSAELVRRLQ DRGAEVKVVM TAAAMEFITP LTLQALSGNP VHTTLLDPEA EAGMGHIELA RWADVILVAP ASADFIARLA SGRGDDLLTT LCLATPAPIA LAPAMNQGMW RDPATQANLD TLRQRGIALF GPAAGEQACG DIGPGRMLEV DEIAELTADL FPNRALDGIK LRITAGPTRE AIDPVRYISN HSSGKMGFAL AAAAADAGAQ VTLISGPVNL ATPERVSRID VSSAQDMYDA SLADLQDCDI FIACAAVADY RPSEAVTQKI KKSADTLTLT LVRNPDIVSS VANSPQRPFT VGFAAETQDV LHYARDKLQR KKLDMIIAND VANTDIGFNS DDNRVVALWN GGEHAFDTMS KAQLSRRLIA LIAEHFRTER D //