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Database: UniProt
Entry: A0A0B3BSL3_9PSED
LinkDB: A0A0B3BSL3_9PSED
Original site: A0A0B3BSL3_9PSED 
ID   A0A0B3BSL3_9PSED        Unreviewed;       835 AA.
AC   A0A0B3BSL3;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Flavodoxin {ECO:0000313|EMBL:KHO63629.1};
GN   ORFNames=PT85_16260 {ECO:0000313|EMBL:KHO63629.1};
OS   Pseudomonas flexibilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=706570 {ECO:0000313|EMBL:KHO63629.1, ECO:0000313|Proteomes:UP000030980};
RN   [1] {ECO:0000313|EMBL:KHO63629.1, ECO:0000313|Proteomes:UP000030980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14085 {ECO:0000313|EMBL:KHO63629.1,
RC   ECO:0000313|Proteomes:UP000030980};
RA   Shin S.-K., Yi H.;
RT   "Genome sequence of Pseudomonas tuomuerensis JCM 14085.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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:KHO63629.1}.
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DR   EMBL; JTAK01000008; KHO63629.1; -; Genomic_DNA.
DR   RefSeq; WP_039607247.1; NZ_JTAK01000008.1.
DR   AlphaFoldDB; A0A0B3BSL3; -.
DR   STRING; 706570.PT85_16260; -.
DR   OrthoDB; 9816402at2; -.
DR   Proteomes; UP000030980; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProt.
DR   CDD; cd06200; SiR_like1; 1.
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; 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; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR005625; PepSY-ass_TM.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR34219:SF3; BLL7967 PROTEIN; 1.
DR   PANTHER; PTHR34219; IRON-REGULATED INNER MEMBRANE PROTEIN-RELATED; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF03929; PepSY_TM; 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   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030980};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        334..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          379..516
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   DOMAIN          529..696
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   835 AA;  92579 MW;  4461148D7A6A1A74 CRC64;
     MFKKTLFQLH WLFGISAGLV LAVMGVTGAL YSFEGEILRL LNSGHGQLAT AEAPRLELGE
     LVARLESSSG ERVVDLRIDD RHAGPATAYL APPPGERRGA RILFDPANGQ VLGTPRGQEF
     FQVVLQLHRW LAMGETGKQI TAASTLMLVF LCLSGLYLRW PRQAGHWRAW LSLDWRKTGR
     GFHWDLHAVA GTWVLPLYLC ASLTGLYWSY DWYRAGLTAL LADPPPAVQA RQPAIDAPAT
     PDYAALWQGI QQAAGPQLIA WNLRLPAAAG QPATVFYILR DAAHVRAFNL LQLDPRSGAI
     VRHERYADKT FTARLLTSVY ALHSGEYFGL PGKVLMLLAS ALMPLFLVTG WLLYLDRRRK
     RRAVRAARST PNAAPGDGWL IGYASQSGFA EQLAWQSASQ LQAAGLAVRV EPLARLDAAS
     LLRHPRALFV LSTFGDGEAP DNARGFERRL LGATLPLDRL AYAVLALGDR HYAQFCAFAR
     RVDAWLERQG GRRLFESVEV DDQDSSALRH WQHQLSELTG TPVPAWHDHR WTGWTLQRRQ
     LLNPGSQGGP VFRLTLTLNG PSDWRAGDIL EIRPRHAQAR VVAWLQRHGG DADEPVELDG
     QPVRLAEALS TRQLPETFAH RVGLHGQALV DSLLPLASRE YSIASIPADG VLELFVRQVR
     HAGDDLGLCS GWLTAHLAEG EQLLGRIRRN SAFHLPADDR PLILIGNGTG LSALRALLRA
     RILVGQRRNW LLFGERQRTH DFHCASELQA ALECGDLQCL DLAFSRDQPD KFYVQDLLRR
     QQDRLRDWLA EGAALYVCGS LDGMAAGVDA TLHELLGAEA VRALVEAGRY RRDVY
//
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