ID V9HYU6_MANES Unreviewed; 707 AA.
AC V9HYU6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Ferric reductase oxidase {ECO:0000313|EMBL:ADR70886.1};
DE EC=1.16.1.7 {ECO:0000313|EMBL:ADR70886.1};
GN Name=FRO1 {ECO:0000313|EMBL:ADR70886.1};
GN ORFNames=MANES_01G254300 {ECO:0000313|EMBL:OAY62259.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:ADR70886.1};
RN [1] {ECO:0000313|EMBL:ADR70886.1}
RP NUCLEOTIDE SEQUENCE.
RA Zou Z.;
RT "Cloning of a cDNA encoding a ferric reductase oxidase (FRO) from Cassava
RT (Manihot esculenta Crantz).";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAY62259.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY62259.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; HQ599253; ADR70886.1; -; mRNA.
DR EMBL; CM004387; OAY62259.1; -; Genomic_DNA.
DR AlphaFoldDB; V9HYU6; -.
DR SMR; V9HYU6; -.
DR STRING; 3983.V9HYU6; -.
DR EnsemblPlants; OAY62259; OAY62259; MANES_01G254300.
DR Gramene; OAY62259; OAY62259; MANES_01G254300.
DR OMA; CTNLHYG; -.
DR OrthoDB; 2671609at2759; -.
DR Proteomes; UP000091857; Chromosome lg1.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0140618; F:ferric-chelate reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IBA:GO_Central.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 2.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR PANTHER; PTHR11972:SF41; FERRIC REDUCTION OXIDASE 2; 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
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 PROSITE; PS51384; FAD_FR; 1.
PE 2: Evidence at transcript level;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ADR70886.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000091857};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 294..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 538..562
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 582..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 317..422
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 707 AA; 79777 MW; E86B62FB0571F9B3 CRC64;
MGSPSHKQTD MLRAAMRLLI ILILLGYLML WFMMPTNTYR HIWLRHVRNK FNSAYFGLQG
ATLVLYSFPI LLIAVLGCVY LHLGKRSDQN DFQSDGRKRS KLSKWKNPMI VKGPLGIVSG
IELGFLFMFV ALLIWSLSTY LHNGFATITP EGGEQVWEAK LDNASLRLGL IGNICLAVLF
FPVTRGSSVL PLFGLTSESS IKHHIWVGHM VMMFFTAHGV GYIIYWAATN QLSEILKWGK
AEISNVAGEL SLLAGLGLWA TTLSSIRRKM FELFFYTHHL YILFMIFFLL HVPISFACIS
LPGFYLFLVD RYLRFLQSRQ RVRSVSARIL PCETLEINFS KTPGLSYNPT SVLFVNVPSI
SKLQWHPFTI TSNSNLESEM LSVVLKSEGS WSKKLYQMLS SPSSIDRLEV SVEGPYGPAS
TQFLRHDTLV MVSGGSGITP FISIIRELIF AATTYKCKTP QVILICAFKN SSYLTMLQLL
LPICGTPSAI SNLQLRIEVY ITREKEPSIN NSKLLRTIWF KPHPTDAPVS AILGPRSWLW
LGAIISSSFV IFLIIIGLIT RYYIYPIDHN TWKVFSYSFR SFLNMLVICI CIAMTASAAV
LRNKKQNERE ANQIQNLEGC TPTRSSPELR LDDAERELES LPHQSIVQDT NVHYGRRPDL
KSILVDCKGS SVGVLVSGPK KMRHEIATIC SSGLASNLHF EFISFSW
//
