ID A0A2K8VPL4_9FLAO Unreviewed; 326 AA. AC A0A2K8VPL4; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 12-OCT-2022, entry version 15. DE RecName: Full=FAD:protein FMN transferase {ECO:0000256|ARBA:ARBA00016337, ECO:0000256|PIRNR:PIRNR006268}; DE EC=2.7.1.180 {ECO:0000256|ARBA:ARBA00011955, ECO:0000256|PIRNR:PIRNR006268}; DE AltName: Full=Flavin transferase {ECO:0000256|PIRNR:PIRNR006268}; GN ORFNames=BTO15_13540 {ECO:0000313|EMBL:AUC23053.1}; OS Polaribacter sejongensis. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Polaribacter. OX NCBI_TaxID=985043 {ECO:0000313|EMBL:AUC23053.1, ECO:0000313|Proteomes:UP000232721}; RN [1] {ECO:0000313|EMBL:AUC23053.1, ECO:0000313|Proteomes:UP000232721} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 23670 {ECO:0000313|EMBL:AUC23053.1, RC ECO:0000313|Proteomes:UP000232721}; RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.; RT "Trade-off between light-utilization and light-protection in marine RT flavobacteria."; RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Flavin transferase that catalyzes the transfer of the FMN CC moiety of FAD and its covalent binding to the hydroxyl group of a CC threonine residue in a target flavoprotein. CC {ECO:0000256|RuleBase:RU363002}. CC -!- CATALYTIC ACTIVITY: CC Reaction=FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + CC H(+); Xref=Rhea:RHEA:36847, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11061, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57692, CC ChEBI:CHEBI:74257, ChEBI:CHEBI:456215; EC=2.7.1.180; CC Evidence={ECO:0000256|ARBA:ARBA00001219, CC ECO:0000256|PIRNR:PIRNR006268, 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. {ECO:0000256|PIRSR:PIRSR006268- CC 2}; CC -!- SIMILARITY: Belongs to the ApbE family. {ECO:0000256|PIRNR:PIRNR006268, CC ECO:0000256|RuleBase:RU363002}. 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; CP019336; AUC23053.1; -; Genomic_DNA. DR Proteomes; UP000232721; Chromosome. 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 Gene3D; 3.10.520.10; -; 1. 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|ARBA:ARBA00022630, KW ECO:0000256|PIRNR:PIRNR006268}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR006268}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR006268}; Signal {ECO:0000256|RuleBase:RU363002}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006268}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|RuleBase:RU363002" FT CHAIN 19..326 FT /note="FAD:protein FMN transferase" FT /evidence="ECO:0000256|RuleBase:RU363002" FT /id="PRO_5014493596" FT BINDING 168 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR006268-2" FT BINDING 280 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR006268-2" FT BINDING 284 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|PIRSR:PIRSR006268-2" SQ SEQUENCE 326 AA; 35627 MW; C3E15C7507819112 CRC64; MKTLLTSFLV LLSIVCAAQT PYKRVLKLMG SRFEITVVAN NEIQGDAYID LVVAEITRIE KLISSWDAHS QTFEINKNAG IKPVKVAPEL FNLIERAIRI SKLTDGAFDI SYASMDKIWK FDGSMKGMPS EETIKASVTK VGIQNIVLDK VHSTVFLKLK GMKIGFGAIG KGYAADKAKA LLISKGAISG IINASGDMNT WGKQPNGTDW KVAITNPMNK NKVFAVFPLN NSAVVTSGNY EKYVNFNGKR YTHIIDPRTG YPSTGIISVT VFAPKAELAD ALSTSVFVMG KQVGLDRINQ LPKIECIIID DTGKITTSKN IEIDKL //