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Database: UniProt
Entry: A0A235G9K2_9NOCA
LinkDB: A0A235G9K2_9NOCA
Original site: A0A235G9K2_9NOCA 
ID   A0A235G9K2_9NOCA        Unreviewed;       438 AA.
AC   A0A235G9K2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Putative ferric reductase {ECO:0000313|EMBL:OYD70259.1};
GN   ORFNames=BDB13_3859 {ECO:0000313|EMBL:OYD70259.1};
OS   Rhodococcus sp. OK302.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1882769 {ECO:0000313|EMBL:OYD70259.1, ECO:0000313|Proteomes:UP000215121};
RN   [1] {ECO:0000313|EMBL:OYD70259.1, ECO:0000313|Proteomes:UP000215121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK302 {ECO:0000313|EMBL:OYD70259.1,
RC   ECO:0000313|Proteomes:UP000215121};
RA   Pelletier D.;
RT   "Populus root and rhizosphere microbial communities from Tennessee, USA.";
RL   Submitted (AUG-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}.
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:OYD70259.1}.
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DR   EMBL; NPJZ01000001; OYD70259.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A235G9K2; -.
DR   OrthoDB; 9801223at2; -.
DR   Proteomes; UP000215121; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR   SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        81..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          203..304
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   438 AA;  48653 MW;  D5B60A8DCEB82BA0 CRC64;
     MTLLSRGIAW IGLYLAVAVI PLVFAVLGHS GPGRGFLTEF SVALGFIGLS MMGMQFALVA
     RFQTAAKPFG EDALVQFHRE ISYVALAFIL AHPILLQVAG IDIVGLLNLA QAPWRARFAV
     TSTVLLLVLI ATSIWRRRMK IRYEVWQVLH GAVSVLVVAF ALAHVFLVGY YVDDAWKKWL
     WAIMTGALIF LLLWVRVIRP LMRLRQPWKI ESVVQERGDA VTLTMVPIGH QGFRFEPGQF
     GWLTVDRSPF SVTSHPFSFS SSAENGTAIS MTIKSLGDFT STVGTISPGT PAYLDGPHGV
     FTPDHNDGPG FVLIAGGVGI TPMMSILRTM ADRRDNRPYL LFYASNSLDD ITFDEELNEL
     KLRLNLTIVH ILRTPPADWT GEQGFLDHDM LARHLPDHHE RLQYFVCGPG PMLDAIENAL
     TELGVPAPHL HTERFIFV
//
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