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Database: UniProt
Entry: A0A2P5DY49_PARAD
LinkDB: A0A2P5DY49_PARAD
Original site: A0A2P5DY49_PARAD 
ID   A0A2P5DY49_PARAD        Unreviewed;       580 AA.
AC   A0A2P5DY49;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   03-MAY-2023, entry version 14.
DE   SubName: Full=Flavodoxin-like {ECO:0000313|EMBL:PON78209.1};
GN   ORFNames=PanWU01x14_021910 {ECO:0000313|EMBL:PON78209.1};
OS   Parasponia andersonii (Sponia andersonii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX   NCBI_TaxID=3476 {ECO:0000313|EMBL:PON78209.1, ECO:0000313|Proteomes:UP000237105};
RN   [1] {ECO:0000313|Proteomes:UP000237105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA   Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA   Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA   Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA   Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA   Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA   Smit S., Geurts R.;
RT   "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT   legume Parasponia.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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:PON78209.1}.
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DR   EMBL; JXTB01000010; PON78209.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5DY49; -.
DR   STRING; 3476.A0A2P5DY49; -.
DR   OrthoDB; 276396at2759; -.
DR   Proteomes; UP000237105; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.360; -; 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; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19384:SF10; NADPH-DEPENDENT DIFLAVIN OXIDOREDUCTASE 1; 1.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237105}.
FT   DOMAIN          7..152
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          174..420
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   580 AA;  65575 MW;  6F7B65E710178B9A CRC64;
     MEDRPKLLTL YASQTGNALD AAEQVAREAD RRGCSVRLLS LDEYDAVALP HETAVVFVVS
     TTGQGDTPDS MKGFWKYLLQ RNLSQHWLEG VHYAVFGLGD SGYQKFNFVA KKLDRRLSDL
     GAVAIVERGF GDDQHPSGFG CMSYLGYVEL NHTEMQIETA QRMSPGKFSR DKNRPECFLK
     LVKNQPLTKE NCGRDVRHFE FEFVSSVVQY EVGGILEVLP TQDRALVDAF IQRCNLDPEA
     FITVHPVEME NYLDTLTNAT VVPIKLKSFV DLTMDVASAS PRRYFFEARI QYVMSNFATA
     AHEKERLQYF ASPEGRDDLY QYNQKERRTV LEVLQDFPSV QMPFEWLVQL VPALKTRAFS
     ISSSLSAHPR QVHLTVSVVT WTTPFKRKRS GLCSTWLSKL DPKQCICIPV WFNKGSLPPP
     TPSLPLILIG PGTGCAPFRG FVEERAIQSA THDTAPVIFF FGCRNEENDY LYRDFWLSHK
     KNGGVLSETK GGGFYVAFSR DQPQKVYVQH KISEHSDRVW SLLSEGAAIY VAGSSTKMPP
     DVLSSFEEII SKESGLPREA AVRWLRALER AGKYHIEAWS
//
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