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Database: UniProt
Entry: A0A239BU63_9ACTN
LinkDB: A0A239BU63_9ACTN
Original site: A0A239BU63_9ACTN 
ID   A0A239BU63_9ACTN        Unreviewed;       469 AA.
AC   A0A239BU63;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Predicted ferric reductase {ECO:0000313|EMBL:SNS10594.1};
GN   ORFNames=SAMN04488107_1393 {ECO:0000313|EMBL:SNS10594.1};
OS   Geodermatophilus saharensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=1137994 {ECO:0000313|EMBL:SNS10594.1, ECO:0000313|Proteomes:UP000198386};
RN   [1] {ECO:0000313|EMBL:SNS10594.1, ECO:0000313|Proteomes:UP000198386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45423 {ECO:0000313|EMBL:SNS10594.1,
RC   ECO:0000313|Proteomes:UP000198386};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FZOH01000002; SNS10594.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239BU63; -.
DR   OrthoDB; 9801223at2; -.
DR   Proteomes; UP000198386; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        27..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          237..337
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   469 AA;  50496 MW;  C4EC46659039EF44 CRC64;
     MSTAVATPSP GTVLTVPEED RRARTDAAVR TVATVLLWAG LALVTWWWAS GGGVADLTAW
     DTGLTSLGRL TGLLASDLLL VQVLLMSRLP VLERAFGQDR LVRLHRVTGL TSFDLLVGHV
     VLVTWGYAAG ELSRTPATLW ELTTQYPGML LAVAGTACLV LVVVTSVRAA RRRLRYQSWH
     LIHLYAYLGV GLALPHQLWT GQEFLSSPAA TVYWWSLWTA AAGAVLVWRV ALPVVRSARH
     GLRVTTVVPE GDGVVSVYLS GRHLDRLPVE AGQFLTWRFL AGPGWTRAHP YSLSAAPDGR
     SLRITVKDSG DGSAAVARLR PGTRALVEGP HGRLSARART RRRVLLVGAG VGVAPLRALA
     EALPYAPGEA ALLYRHTGRP LFERELAVLA RERGLQVLLL PGHRRSPDSW LGEGVPPVPD
     AAVLAAWVPD LADRDVYVCG PEGWAAGVRR SAEAAGLPAG RCHVESFGW
//
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