ID A0A1V8RN73_9RHIZ Unreviewed; 247 AA. AC A0A1V8RN73; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 05-DEC-2018, entry version 7. DE RecName: Full=FAD:protein FMN transferase {ECO:0000256|RuleBase:RU363002}; DE EC=2.7.1.180 {ECO:0000256|RuleBase:RU363002}; GN ORFNames=BFN67_20975 {ECO:0000313|EMBL:OQM74640.1}; OS Pseudaminobacter manganicus. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Phyllobacteriaceae; Pseudaminobacter. OX NCBI_TaxID=1873176 {ECO:0000313|EMBL:OQM74640.1, ECO:0000313|Proteomes:UP000191905}; RN [1] {ECO:0000313|EMBL:OQM74640.1, ECO:0000313|Proteomes:UP000191905} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JH-7 {ECO:0000313|EMBL:OQM74640.1, RC ECO:0000313|Proteomes:UP000191905}; RX PubMed=28036252; RA Li J., Huang J., Liao S., Wang G.; RT "Pseudaminobacter manganicus sp. nov., isolated from sludge of a RT manganese mine."; RL Int. J. Syst. Evol. Microbiol. 0:0-0(2016). 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|RuleBase:RU363002}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU363002}; CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000256|RuleBase:RU363002}. CC -!- SIMILARITY: Belongs to the ApbE family. CC {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:OQM74640.1}. 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; MDET01000025; OQM74640.1; -; Genomic_DNA. DR Proteomes; UP000191905; Unassembled WGS sequence. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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:InterPro. DR InterPro; IPR024932; ApbE. DR InterPro; IPR003374; ApbE-like_sf. DR PANTHER; PTHR30040; PTHR30040; 2. DR Pfam; PF02424; ApbE; 2. DR SUPFAM; SSF143631; SSF143631; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|RuleBase:RU363002}; KW Cell membrane {ECO:0000256|RuleBase:RU363002}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000191905}; KW FAD {ECO:0000256|RuleBase:RU363002}; KW Flavoprotein {ECO:0000256|RuleBase:RU363002}; KW Lipoprotein {ECO:0000256|RuleBase:RU363002}; KW Magnesium {ECO:0000256|RuleBase:RU363002}; KW Membrane {ECO:0000256|RuleBase:RU363002}; KW Metal-binding {ECO:0000256|RuleBase:RU363002}; KW Reference proteome {ECO:0000313|Proteomes:UP000191905}; KW Transferase {ECO:0000256|RuleBase:RU363002}. FT COILED 58 78 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 247 AA; 26870 MW; D6E40BDEF9B06461 CRC64; MRETRILMGM PVTVDIGDTS SGALIDTVFA YFERIDRRFS TYRADSEISA INRGDVPVKN WSDEMMEVLA LAEQTRNETD GYFDIRKPDG SLDPSGIVKG WAIRNAAATV RRTGVNGFFI EAGGDIQSCG RNASGLDWSV GIRNPFNTDE IIKILYPRGR GVATSGTYIR GQHIYNPHEA GDTITDIVSV TVVGSDVLEA DRFATAAFAM GRNGIFFIEQ TPGLEGYVVD SNGRATPTSG FGAFCRS //