ID   APBEF_RHOCA             Reviewed;         523 AA.
AC   Q52718;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
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   AltName: Full=Nitrogen fixation protein RnfF {ECO:0000303|PubMed:8264535};
GN   Name=rnfF {ECO:0000303|PubMed:8264535};
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=B10S;
RX   PubMed=8264535; DOI=10.1007/bf00279903;
RA   Schmehl M., Jahn A., Meyer zu Vilsendorf A., Hennecke S., Masepohl B.,
RA   Schuppler M., Marxer M., Oelze J., Klipp W.;
RT   "Identification of a new class of nitrogen fixation genes in Rhodobacter
RT   capsulatus: a putative membrane complex involved in electron transport to
RT   nitrogenase.";
RL   Mol. Gen. Genet. 241:602-615(1993).
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 (By similarity). Is likely
CC       involved in the modification of RnfG and RnfD. Required for nitrogen
CC       fixation (PubMed:8264535). {ECO:0000250|UniProtKB:A5F5Y3,
CC       ECO:0000269|PubMed:8264535, ECO:0000305}.
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 membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the RseC family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the ApbE family.
CC       {ECO:0000305}.
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DR   EMBL; X72888; CAA51405.1; -; Genomic_DNA.
DR   PIR; S39899; S39899.
DR   AlphaFoldDB; Q52718; -.
DR   SMR; Q52718; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0009399; P:nitrogen fixation; 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   SUPFAM; SSF143631; SSF143631; 1.
PE   3: Inferred from homology;
KW   Cell membrane; FAD; Flavoprotein; Magnesium; Membrane; Metal-binding;
KW   Nitrogen fixation; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..523
FT                   /note="FAD:protein FMN transferase"
FT                   /id="PRO_0000097379"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         277..279
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O83774"
FT   BINDING         336
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O83774"
FT   BINDING         339
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O83774"
FT   BINDING         342
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O83774"
FT   BINDING         423..425
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:O83774"
FT   BINDING         450
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O83774"
FT   BINDING         454
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O83774"
SQ   SEQUENCE   523 AA;  54143 MW;  560F0F5722759613 CRC64;
     MTGCCDDGPA TGPRDLRERL RVVAVRGESL VVAADRASAC AACAEAKGCG TRALMSMHRT
     DLMTIARPAG LIVAPGDEVE VAMSGNNLLA GAGLAYLLPA LAFVVALALA SGAGLSDGGA
     ALVGGVVLMF SFLPLVLLEA ARGCRGRCRC STCIRGTADD GRRAAFRTGL ALAAGLVLAG
     GVRVLTAPAP DVSETFYVFG TLLEVETHGV PEAQARDAMA VLGAHFRQMH RDWHAWAPGE
     LESLNAAMAA GQSFEVDPGL AKLLQQGRDL ACRSEGLFDP AVGGMVEAWG FHADTPPEAI
     RSDAVVAKLL AGAPKMTDLT ITGTTVRSSN PAVQLDLGAY AKGAALDLAE ADLTAAGIRD
     AVLNAGGGVQ VLGDHGSRPW RVAIRDPFEW GVVGAVSLRP GEALHTSGNY ERYFDRGGIR
     FSHIIDPRTA RPMRGVVSVS VLSDNGALSD AAATALCVAG EEDWPRIAAQ MGVRAVLRIT
     DDGSIFATPE MRARLEAVEG GFPAPITVVD LPKDVAIPLC PEG