ID E2NUZ7_9FIRM Unreviewed; 159 AA. AC E2NUZ7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 11-JAN-2011, entry version 2. DE RecName: Full=Phosphopantetheine adenylyltransferase; DE EC=2.7.7.3; DE AltName: Full=Dephospho-CoA pyrophosphorylase; DE AltName: Full=Pantetheine-phosphate adenylyltransferase; GN Name=coaD; ORFNames=CATMIT_02428; OS Catenibacterium mitsuokai DSM 15897. OC Bacteria; Firmicutes; Erysipelotrichi; Erysipelotrichales; OC Erysipelotrichaceae; Catenibacterium. OX NCBI_TaxID=451640; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15897; RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'- CC phosphopantetheine, yielding dephospho-CoA (dPCoA) and CC pyrophosphate (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + pantetheine 4'-phosphate = diphosphate + CC 3'-dephospho-CoA. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 4/5. CC -!- SUBUNIT: Homohexamer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the bacterial CoaD family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. 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; ACCK01000415; EEF92966.1; -; Genomic_DNA. DR HAMAP; MF_00151; PPAT_bact; 1; -. DR InterPro; IPR004821; Cyt_trans-rel. DR InterPro; IPR004820; Cytidylyltransf. DR InterPro; IPR001980; LPS_biosynth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR Pfam; PF01467; CTP_transf_2; 1. DR PRINTS; PR01020; LPSBIOSNTHSS. DR TIGRFAMs; TIGR01510; coaD_prev_kdtB; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. PE 3: Inferred from homology; KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Nucleotide-binding; KW Nucleotidyltransferase; Transferase. SQ SEQUENCE 159 AA; 18147 MW; B52D4B38D1FAC441 CRC64; MIKAVYTGTF DPVTNGHLDI IERASKMYDV LYVTIFINPH KTCLFSVEER IEMLREATKQ FPNVVIDESS ALAVEYAREV GAQVLVRGLR ATEDYNYESL MCFTNQYLDE GIETVFLMTR LAYTFVSSSF VKEIVSHNHS VEGLVPACVE EKLIKKYRG //