ID   APBE_BUCBP              Reviewed;         341 AA.
AC   Q89AP6;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=FAD:protein FMN transferase {ECO:0000250|UniProtKB:A5F5Y3};
DE            EC=2.7.1.180 {ECO:0000250|UniProtKB:A5F5Y3};
DE   AltName: Full=Flavin transferase {ECO:0000250|UniProtKB:A5F5Y3};
DE   Flags: Precursor;
GN   Name=apbE; OrderedLocusNames=bbp_209;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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 such as NqrB and NqrC, two
CC       subunits of the NQR complex. {ECO:0000250|UniProtKB:A5F5Y3}.
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:0000250|UniProtKB:A5F5Y3};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A5F5Y3};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P41780, ECO:0000255|PROSITE-ProRule:PRU00303};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P41780, ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Periplasmic side {ECO:0000250|UniProtKB:P41780}.
CC   -!- SIMILARITY: Belongs to the ApbE family. {ECO:0000305}.
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DR   EMBL; AE016826; AAO26941.1; -; Genomic_DNA.
DR   RefSeq; WP_011091342.1; NC_004545.1.
DR   AlphaFoldDB; Q89AP6; -.
DR   SMR; Q89AP6; -.
DR   STRING; 224915.bbp_209; -.
DR   EnsemblBacteria; AAO26941; AAO26941; bbp_209.
DR   GeneID; 56470751; -.
DR   KEGG; bab:bbp_209; -.
DR   eggNOG; COG1477; Bacteria.
DR   HOGENOM; CLU_044403_0_0_6; -.
DR   OMA; LINIWGF; -.
DR   OrthoDB; 2021063at2; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017013; P:protein flavinylation; IEA:InterPro.
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   Cell inner membrane; Cell membrane; FAD; Flavoprotein; Lipoprotein;
KW   Magnesium; Membrane; Metal-binding; Reference proteome; Signal;
KW   Transferase.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..341
FT                   /note="FAD:protein FMN transferase"
FT                   /id="PRO_0000001753"
FT   BINDING         36
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         73
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         114..116
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         176
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         179
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB85"
FT   BINDING         182
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         266
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P41780"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O83774"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB85"
FT   BINDING         296
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O83774"
SQ   SEQUENCE   341 AA;  38686 MW;  5D78535CC9DE4602 CRC64;
     MAYVINICIL YFLIISIQIN KVQKKYETVF LCGYTMGTTW KVKIINNRHL TYYNLKKKIE
     KQLCYDNNQI SSWNKNSDIS NFNKNFTTKP QKINKNLAKL ISIGLLVGKK TNNLLDITSG
     TLINIWGFGP TSRKHSIPSK KTIKLAQMLT GLNHIKLLIN KQQYYLQKDI PKLQINLSTL
     GEGFAADNLK RILDDEGIND YYISIGGTVV THTSPKNSQN KIIAIQKPTE TDNEIHCLIS
     LKNNAVSTSG TYRNYYTLHK KIIHIINPIT GNPANTDLVS VTVISKSALK SDAWDTGLIL
     LGFRQAKKIS IQEKLAVCLI KKNKSTLFTW TSPQFKKFLI K