ID   A0A1V8RN73_9RHIZ        Unreviewed;       247 AA.
AC   A0A1V8RN73;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   30-AUG-2017, entry version 3.
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: FAD + [protein]-L-threonine = [protein]-FMN-L-
CC       threonine + AMP. {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}.
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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.
DR   PANTHER; PTHR30040; PTHR30040; 1.
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   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}.
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
//