ID A0A318MQL9_9LACO Unreviewed; 273 AA. AC A0A318MQL9; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 16-JAN-2019, entry version 4. 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 ORFNames=DK873_00585 {ECO:0000313|EMBL:PXY86271.1}; OS Lactobacillus melliventris. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1218507 {ECO:0000313|EMBL:PXY86271.1, ECO:0000313|Proteomes:UP000247698}; RN [1] {ECO:0000313|EMBL:PXY86271.1, ECO:0000313|Proteomes:UP000247698} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ESL0184 {ECO:0000313|EMBL:PXY86271.1, RC ECO:0000313|Proteomes:UP000247698}; RA Ellegaard K.M.; RT "Reference genomes for bee gut microbiota database."; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-dephospho-CoA + ATP = 2'-(5''-triphospho-alpha-D- CC ribosyl)-3'-dephospho-CoA + adenine; Xref=Rhea:RHEA:15117, CC ChEBI:CHEBI:16708, ChEBI:CHEBI:30616, ChEBI:CHEBI:57328, CC ChEBI:CHEBI:61378; EC=2.4.2.52; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00397, 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 CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PXY86271.1}. 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; QGLG01000001; PXY86271.1; -; Genomic_DNA. DR Proteomes; UP000247698; 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}; KW Complete proteome {ECO:0000313|Proteomes:UP000247698}; KW 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}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 248 268 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 273 AA; 30112 MW; 531C195BA5A88235 CRC64; MTNSITQNAL RSLLYEVVTE PKPGLVDPGS PGPHPDMDIY TFIDSSISLE SYFATAVKIG QTFHSTDLTQ MFQQLRQRGI TAEKEMFTAT HGANTHKGAI FALGIFVCAE SYSMTNKTEL FLTITKMCKG LVQHDLVQNN ELQTAGEQEF VKYKIGGARA QAEQGYPIVR EVALPFLKSS TGTVQTRLLD TLMKIATIVV DSNLIKRAGN YDVVKWLHQE ATKYLDLGGY AAAAGKKQLQ KLSKECLVHN YSLGGCADLL IVTIFVAFER GYI //