ID A0A2V4V6C3_9GAMM Unreviewed; 462 AA. AC A0A2V4V6C3; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 10-OCT-2018, entry version 2. 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 RT genomes of soil and plant-associated and newly described type RT strains."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes two steps in the biosynthesis of coenzyme A. CC In the first step cysteine is conjugated to 4'-phosphopantothenate CC to form 4-phosphopantothenoylcysteine, in the latter compound is CC decarboxylated to form 4'-phosphopantotheine. CC {ECO:0000256|RuleBase:RU364078}. CC -!- CATALYTIC ACTIVITY: CTP + (R)-4'-phosphopantothenate + L-cysteine CC = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine. CC {ECO:0000256|RuleBase:RU364078}. CC -!- CATALYTIC ACTIVITY: N-((R)-4'-phosphopantothenoyl)-L-cysteine = CC pantotheine 4'-phosphate + CO(2). {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 CC (R)-pantothenate: step 2/5. {ECO:0000256|RuleBase:RU364078}. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 3/5. {ECO:0000256|RuleBase:RU364078}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PPC CC synthetase 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 CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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; 2. DR SUPFAM; SSF52507; SSF52507; 1. DR TIGRFAMs; TIGR00521; coaBC_dfp; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000247746}; KW Decarboxylase {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|RuleBase:RU364078}. FT DOMAIN 3 173 Flavoprotein. {ECO:0000259|Pfam:PF02441}. FT DOMAIN 185 266 DFP. {ECO:0000259|Pfam:PF04127}. FT DOMAIN 316 423 DFP. {ECO:0000259|Pfam:PF04127}. 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 //