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Database: UniProt
Entry: A0A0N1GB71_9ACTN
LinkDB: A0A0N1GB71_9ACTN
Original site: A0A0N1GB71_9ACTN 
ID   A0A0N1GB71_9ACTN        Unreviewed;       450 AA.
AC   A0A0N1GB71;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Ferric reductase domain protein transmembrane component domain-containing protein {ECO:0000313|EMBL:KPI16382.1};
GN   ORFNames=OK074_1994 {ECO:0000313|EMBL:KPI16382.1};
OS   Actinobacteria bacterium OK074.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI16382.1, ECO:0000313|Proteomes:UP000037991};
RN   [1] {ECO:0000313|EMBL:KPI16382.1, ECO:0000313|Proteomes:UP000037991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK074 {ECO:0000313|EMBL:KPI16382.1,
RC   ECO:0000313|Proteomes:UP000037991};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT   and OV320.";
RL   Submitted (AUG-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPI16382.1}.
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DR   EMBL; LJCV01000099; KPI16382.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1GB71; -.
DR   PATRIC; fig|1592327.3.peg.2980; -.
DR   OrthoDB; 9801223at2; -.
DR   Proteomes; UP000037991; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd06198; FNR_like_3; 1.
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; IPR001433; OxRdtase_FAD/NAD-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   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
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   Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        25..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        53..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        98..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        168..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          227..327
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   450 AA;  49370 MW;  1FC9AB12509F4C23 CRC64;
     MTTVHEPRTA THVPLPPRRS PPPPVLALLW AGAAAVLALW WSDTGSVVGA AGWLTGAGRI
     AGLLCGYACA VLVALMARVP LFERRIGSDR VARWHAMAGR YTVCLLLAHV VLILLGYAAQ
     DHASLVHETV TVVLDYPDML KATIGTLILF AVGISSARAA RRRIGHEFWY YVHLLTYVAV
     FLAFWHQLTL GSDFTGNRAA QLAWYALYLG VTALVLWFRV LAPVRLNLRH RLRVESVHRE
     APGVWSVVMS GHQLDRMGAE SGQFFRWRFL TEGMRWTSTP YSLSAPPRAG RLRITVKALG
     DHSASVALLR PGTRVWAEGP YGALTAERRT AQKVLLIAGG VGVTPLRALF ETLPGDVTLL
     YRARTAEDLA LGRELEAIAR WRGGRVLYAL NGSRGERPEF TAQSLRAAVP GIGGHDVYLC
     GPHGFAREVY AALRAAGVPD RRIHHESFEL
//
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