ID A0A1Q5K5R1_9ACTN Unreviewed; 450 AA.
AC A0A1Q5K5R1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Ferric reductase {ECO:0000313|EMBL:OKJ76888.1};
GN ORFNames=AMK32_32745 {ECO:0000313|EMBL:OKJ76888.1};
OS Streptomyces sp. CB01883.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703943 {ECO:0000313|EMBL:OKJ76888.1, ECO:0000313|Proteomes:UP000186398};
RN [1] {ECO:0000313|EMBL:OKJ76888.1, ECO:0000313|Proteomes:UP000186398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01883 {ECO:0000313|EMBL:OKJ76888.1,
RC ECO:0000313|Proteomes:UP000186398};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ76888.1}.
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DR EMBL; LIWA01000008; OKJ76888.1; -; Genomic_DNA.
DR RefSeq; WP_073899559.1; NZ_LIWA01000008.1.
DR AlphaFoldDB; A0A1Q5K5R1; -.
DR OrthoDB; 9801223at2; -.
DR Proteomes; UP000186398; 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 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:UP000186398};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..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..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..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"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 48734 MW; 8974A83AF3CBD1AD CRC64;
MTTVETGRSA PPRRGTARPS PAGPVLAVLW AGAAAVVALW WTDTGAVVGT AGVLTGAGRI
AGLLCGYACA VLVGLMARVP LLETRIGSDR VARWHAMAGR YTVCLLLAHV TLILAGYAAQ
DRVSWWHETV TVVLDYPDML KATAGTVILF VVGVTSVRAA RRRVRHEFWY YVHLLTYAAV
FLAFFHQLTL GEQFAGSTVA TALWYVLYLG VAALVVWFRI LAPVRLNRRH RLRVDSVHRE
APGVHSVVVR GRHLDELGAL PGQFFRWRFL ADGMGWTSTP YSLSAPPRPG MLRVTVKALG
DHSAAVPLLR PGTRVWAEGP YGSLTAGRAT GHRSLLIAAG VGVTPLRALF ETLPGEVTLL
YRARSAEDLA LGGELEAIAR WRGARVLYAL NGPRGERPPV TAESLRAAVP GLPGHDVYVC
GPHGFARDVY EALRAAGVPD RRIHHESFEL
//
