ID E2NUZ7_9FIRM Unreviewed; 159 AA. AC E2NUZ7; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 16-SEP-2015, entry version 29. DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS00109024}; DE EC=2.7.7.3 {ECO:0000256|HAMAP-Rule:MF_00151, ECO:0000256|SAAS:SAAS00109037}; DE AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000256|HAMAP-Rule:MF_00151}; DE AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00151}; GN Name=coaD {ECO:0000256|HAMAP-Rule:MF_00151, GN ECO:0000313|EMBL:EEF92966.1}; GN ORFNames=CATMIT_02428 {ECO:0000313|EMBL:EEF92966.1}; OS Catenibacterium mitsuokai DSM 15897. OC Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales; OC Erysipelotrichaceae; Catenibacterium. OX NCBI_TaxID=451640 {ECO:0000313|EMBL:EEF92966.1}; RN [1] {ECO:0000313|EMBL:EEF92966.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DSM 15897 {ECO:0000313|EMBL:EEF92966.1}; 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. {ECO:0000256|HAMAP-Rule:MF_00151, CC ECO:0000256|SAAS:SAAS00109030}. CC -!- CATALYTIC ACTIVITY: ATP + pantetheine 4'-phosphate = diphosphate + CC 3'-dephospho-CoA. {ECO:0000256|HAMAP-Rule:MF_00151, CC ECO:0000256|SAAS:SAAS00109039}. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00151, CC ECO:0000256|SAAS:SAAS00108991}. CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00151, CC ECO:0000256|SAAS:SAAS00109038}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00151, CC ECO:0000256|SAAS:SAAS00108990}. CC -!- SIMILARITY: Belongs to the bacterial CoaD family. CC {ECO:0000256|HAMAP-Rule:MF_00151}. 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:EEF92966.1}. 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; ACCK01000415; EEF92966.1; -; Genomic_DNA. DR EnsemblBacteria; EEF92966; EEF92966; CATMIT_02428. DR PATRIC; 30396371; VBICatMit90418_1759. DR UniPathway; UPA00241; UER00355. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00151; PPAT_bact; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR001980; LPS_biosynth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_like; 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 {ECO:0000256|HAMAP-Rule:MF_00151, KW ECO:0000256|SAAS:SAAS00109018}; KW Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00151, KW ECO:0000256|SAAS:SAAS00109017}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00151, KW ECO:0000256|SAAS:SAAS00109028}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00151, KW ECO:0000256|SAAS:SAAS00109023}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00151, KW ECO:0000256|SAAS:SAAS00109019}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00151, KW ECO:0000256|SAAS:SAAS00108989}. SQ SEQUENCE 159 AA; 18147 MW; B52D4B38D1FAC441 CRC64; MIKAVYTGTF DPVTNGHLDI IERASKMYDV LYVTIFINPH KTCLFSVEER IEMLREATKQ FPNVVIDESS ALAVEYAREV GAQVLVRGLR ATEDYNYESL MCFTNQYLDE GIETVFLMTR LAYTFVSSSF VKEIVSHNHS VEGLVPACVE EKLIKKYRG //