ID A0A352P741_9FIRM Unreviewed; 357 AA. AC A0A352P741; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 05-DEC-2018, entry version 2. 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; 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. 0:0-0(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, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30013, ChEBI:CHEBI:456215, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:74257, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11061; 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|RuleBase:RU363002}; 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:0016740; F:transferase activity; IEA:UniProtKB-KW. 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|RuleBase:RU363002}; KW Flavoprotein {ECO:0000256|PIRNR:PIRNR006268, KW ECO:0000256|RuleBase:RU363002}; KW Magnesium {ECO:0000256|PIRNR:PIRNR006268, KW ECO:0000256|RuleBase:RU363002}; KW Metal-binding {ECO:0000256|PIRNR:PIRNR006268, KW 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. 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 //