ID A0A0F4M651_9LACO Unreviewed; 273 AA. AC A0A0F4M651; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 11-DEC-2019, entry version 15. DE RecName: Full=Probable 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase {ECO:0000256|HAMAP-Rule:MF_00397}; DE Short=2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase {ECO:0000256|HAMAP-Rule:MF_00397}; DE EC=2.4.2.52 {ECO:0000256|HAMAP-Rule:MF_00397}; GN Name=citG {ECO:0000256|HAMAP-Rule:MF_00397, GN ECO:0000313|EMBL:KJY66043.1}; GN ORFNames=JF73_01100 {ECO:0000313|EMBL:KJY66043.1}; OS Lactobacillus helsingborgensis. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1218494 {ECO:0000313|EMBL:KJY66043.1, ECO:0000313|Proteomes:UP000033563}; RN [1] {ECO:0000313|EMBL:KJY66043.1, ECO:0000313|Proteomes:UP000033563} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bma5 {ECO:0000313|EMBL:KJY66043.1, RC ECO:0000313|Proteomes:UP000033563}; RA Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G., RA Vasquez A.; RT "Comparative genomics of the lactic acid bacteria isolated from the honey RT bee gut."; RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D-ribosyl)- CC 3'-dephospho-CoA + adenine; Xref=Rhea:RHEA:15117, ChEBI:CHEBI:16708, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57328, ChEBI:CHEBI:61378; EC=2.4.2.52; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00397, CC ECO:0000256|SAAS:SAAS01125469}; CC -!- SIMILARITY: Belongs to the CitG/MdcB family. {ECO:0000256|HAMAP- CC Rule:MF_00397}. 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:KJY66043.1}. 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; JXJR01000002; KJY66043.1; -; Genomic_DNA. DR RefSeq; WP_046326553.1; NZ_KQ034046.1. DR EnsemblBacteria; KJY66043; KJY66043; JF73_01100. DR PATRIC; fig|1218494.3.peg.244; -. DR Proteomes; UP000033563; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016310; P:phosphorylation; IEA:InterPro. DR HAMAP; MF_00397; CitG; 1. DR InterPro; IPR002736; CitG. DR InterPro; IPR017551; TriPribosyl-deP-CoA_syn_CitG. DR PANTHER; PTHR30201; PTHR30201; 1. DR Pfam; PF01874; CitG; 1. DR TIGRFAMs; TIGR03125; citrate_citG; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00397, KW ECO:0000256|SAAS:SAAS01057247}; Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00397, KW ECO:0000256|SAAS:SAAS01057252}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00397, KW ECO:0000256|SAAS:SAAS01057253}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 248..268 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 273 AA; 29833 MW; 20D1A252EFC3C56B CRC64; MTNSITTNAL RALLYEVVTE PKPGLVNPAS SGPHPDMDIY TFIDSSLSLE SYFAAAVQIG QNFSATDLTK MFQQLRKRGI IAEKEMFTAT HGVNTHKGAI FALGICACAE SYSAVNNTEL FLTITQMCRG LVHHDLVENN QLQTAGEKEF IQYQIGGARA QAEQGYPVVR EVALPFLKNS TGTLQARLID TLIKIAAVSV DSNLIKRAGN YSVIKWLHAG ATKYLALGGY QTLAGRKQLQ KLCRDCLIHN YSLGGCADLL IVTIFVALQR GYI //