ID A0A352P741_9FIRM Unreviewed; 357 AA. AC A0A352P741; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 16-JAN-2019, entry version 3. DE RecName: Full=FAD:protein FMN transferase {ECO:0000256|PIRNR:PIRNR006268, ECO:0000256|RuleBase:RU363002}; DE EC=2.7.1.180 {ECO:0000256|PIRNR:PIRNR006268, ECO:0000256|RuleBase:RU363002}; DE AltName: Full=Flavin transferase {ECO:0000256|PIRNR:PIRNR006268}; GN ORFNames=DC053_17755 {ECO:0000313|EMBL:HBD00775.1}; OS Lachnoclostridium sp. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae. OX NCBI_TaxID=2028282 {ECO:0000313|EMBL:HBD00775.1}; RN [1] {ECO:0000313|EMBL:HBD00775.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA11745 {ECO:0000313|EMBL:HBD00775.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny RT substantially revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). CC -!- FUNCTION: Flavin transferase that catalyzes the transfer of the CC FMN moiety of FAD and its covalent binding to the hydroxyl group CC of a threonine residue in a target flavoprotein. CC {ECO:0000256|RuleBase:RU363002}. CC -!- CATALYTIC ACTIVITY: CC Reaction=FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl- CC [protein] + H(+); Xref=Rhea:RHEA:36847, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11061, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:57692, ChEBI:CHEBI:74257, ChEBI:CHEBI:456215; CC EC=2.7.1.180; Evidence={ECO:0000256|PIRNR:PIRNR006268, CC ECO:0000256|RuleBase:RU363002}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR006268-2}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR006268-2}; CC Note=Magnesium. Can also use manganese. CC {ECO:0000256|PIRSR:PIRSR006268-2}; CC -!- SIMILARITY: Belongs to the ApbE family. CC {ECO:0000256|PIRNR:PIRNR006268, ECO:0000256|RuleBase:RU363002}. 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:HBD00775.1}. 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; DNNH01000217; HBD00775.1; -; Genomic_DNA. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0017013; P:protein flavinylation; IEA:UniProtKB-UniRule. DR InterPro; IPR024932; ApbE. DR InterPro; IPR003374; ApbE-like_sf. DR PANTHER; PTHR30040; PTHR30040; 1. DR Pfam; PF02424; ApbE; 1. DR PIRSF; PIRSF006268; ApbE; 1. DR SUPFAM; SSF143631; SSF143631; 1. PE 3: Inferred from homology; KW FAD {ECO:0000256|PIRNR:PIRNR006268, ECO:0000256|PIRSR:PIRSR006268-1, KW ECO:0000256|RuleBase:RU363002}; KW Flavoprotein {ECO:0000256|PIRNR:PIRNR006268, KW ECO:0000256|RuleBase:RU363002}; KW Magnesium {ECO:0000256|PIRNR:PIRNR006268, KW ECO:0000256|PIRSR:PIRSR006268-2, ECO:0000256|RuleBase:RU363002}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR006268, KW ECO:0000256|PIRSR:PIRSR006268-2, ECO:0000256|RuleBase:RU363002}; KW Signal {ECO:0000256|RuleBase:RU363002}; KW Transferase {ECO:0000256|PIRNR:PIRNR006268, KW ECO:0000256|RuleBase:RU363002, ECO:0000313|EMBL:HBD00775.1}. FT SIGNAL 1 30 {ECO:0000256|RuleBase:RU363002}. FT CHAIN 31 357 FAD:protein FMN transferase. FT {ECO:0000256|RuleBase:RU363002}. FT /FTId=PRO_5016485185. FT NP_BIND 126 128 FAD. {ECO:0000256|PIRSR:PIRSR006268-1}. FT NP_BIND 191 193 FAD. {ECO:0000256|PIRSR:PIRSR006268-1}. FT METAL 194 194 Magnesium; via carbonyl oxygen. FT {ECO:0000256|PIRSR:PIRSR006268-2}. FT METAL 308 308 Magnesium. {ECO:0000256|PIRSR: FT PIRSR006268-2}. FT METAL 312 312 Magnesium. {ECO:0000256|PIRSR: FT PIRSR006268-2}. FT BINDING 197 197 FAD. {ECO:0000256|PIRSR:PIRSR006268-1}. FT BINDING 281 281 FAD. {ECO:0000256|PIRSR:PIRSR006268-1}. FT BINDING 283 283 FAD. {ECO:0000256|PIRSR:PIRSR006268-1}. SQ SEQUENCE 357 AA; 39776 MW; 3F21B1E1B9342D63 CRC64; MQNKKAVKFL IIAGSLAALT MAAVNTAAIG AKKDQRFHAE FLKLFDTVTQ IVGYAKNKEE FTQITTDIHD ELEIYHELYD IYNDYDGINN IKTINDNAGK SPVKVDQKII DMLKAAEEAY EKTDGKVNVA MGSVLSIWHD YRTKGIDNPE TAQVPPMDKL KEAALHTDFS KVIVDEDAST VYLEDPDMSL DVGAIAKGYA TERVARFLEA KGIDHVLLSV GGNIRAIGIR ADGKPWKLDI QNPDLDSDKK SIDTLDLNGF SLVSSGDYER FYIVDGVRYH HIIDPVTLMP AAYFRAVSIV CKDSEWADAL STAIFNMPYE EGLAMIEDMK GVEAMWVLPD STIKTSSGYE AYRDHDR //