ID A0A2V4V6C3_9GAMM Unreviewed; 462 AA. AC A0A2V4V6C3; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 12-AUG-2020, entry version 8. 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 ORFNames=DFP82_11059 {ECO:0000313|EMBL:PYE37978.1}; OS Psychrobacter fozii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=198480 {ECO:0000313|EMBL:PYE37978.1, ECO:0000313|Proteomes:UP000247746}; RN [1] {ECO:0000313|EMBL:PYE37978.1, ECO:0000313|Proteomes:UP000247746} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CECT 5889 {ECO:0000313|EMBL:PYE37978.1, RC ECO:0000313|Proteomes:UP000247746}; RA Whitman W.; RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of RT soil and plant-associated and newly described type strains."; RL Submitted (JUN-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 = CO2 + D- CC pantetheine 4'-phosphate; 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:PYE37978.1}. 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; QJSU01000010; PYE37978.1; -; Genomic_DNA. DR UniPathway; UPA00241; UER00353. DR Proteomes; UP000247746; 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; -; 2. DR Gene3D; 3.40.50.1950; -; 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; 2. 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, 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:PYE37978.1}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU364078}. FT DOMAIN 3..173 FT /note="Flavoprotein" FT /evidence="ECO:0000259|Pfam:PF02441" FT DOMAIN 185..266 FT /note="DFP" FT /evidence="ECO:0000259|Pfam:PF04127" FT DOMAIN 316..423 FT /note="DFP" FT /evidence="ECO:0000259|Pfam:PF04127" FT REGION 280..305 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 462 AA; 49660 MW; 5630A9ECCAAB3670 CRC64; MSNIVLAITG GIAAYKSAIF ARLLIKAGFN VRVIMTTGAQ AFITPLTLQA LTGNEVHISL LDEQAEAGMG HIELAKWADL IVIAPASANT LARLAMGMAD DLLTTVCLAT TAPVIVAPAM NQQMWAHPAV NLNVQTLGDM NYHVIQPASG EQACGDVGAG RLPEPEELLA EVLLFNAMQT TPQLLAGKRV VITAGPTVEA IDPVRYLSNH STGKMGFALA RACVAAGAEV ILITGGKVAL PTPLKVTRID VLSAQDMLTA AQQCVDGTHS ELQYISEDEH DHDHDHGHHH DHSHEHSHDH HGDCDCGDEQ DDVTVSTDDN VRVADIFIAT AAVADYRTEE AAPQKIKKTQ DAMALKLVKN PDILATISLA HPELFVVGFA AETQDVEHYA RGKLISKNLD LIACNDVSRA DIGFASDDNA MQVFFSERYE NDSVMLEKAS KDKIAEQLAS IIGETVWQRH NS //