ID F0RFT3_CELLC Unreviewed; 733 AA.
AC F0RFT3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Oxidoreductase FAD/NAD(P)-binding domain protein {ECO:0000313|EMBL:ADY30058.1};
GN OrderedLocusNames=Celly_2238 {ECO:0000313|EMBL:ADY30058.1};
OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS NCIMB 1423 / VKM B-1433 / Cy l20).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY30058.1, ECO:0000313|Proteomes:UP000007487};
RN [1] {ECO:0000313|EMBL:ADY30058.1, ECO:0000313|Proteomes:UP000007487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX PubMed=21677859; DOI=10.4056/sigs.1774329;
RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Ivanova N.;
RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL Stand. Genomic Sci. 4:221-232(2011).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR EMBL; CP002534; ADY30058.1; -; Genomic_DNA.
DR RefSeq; WP_013621802.1; NC_015167.1.
DR AlphaFoldDB; F0RFT3; -.
DR STRING; 867900.Celly_2238; -.
DR KEGG; cly:Celly_2238; -.
DR eggNOG; COG0369; Bacteria.
DR eggNOG; COG3182; Bacteria.
DR HOGENOM; CLU_001570_17_4_10; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000007487; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; IPR008254; Flavodoxin/NO_synth.
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; PTHR19384:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF03929; PepSY_TM; 1.
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 Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007487};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 130..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 340..479
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 494..594
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 733 AA; 82667 MW; B6C2E4ED62485E6E CRC64;
MTLSVWRYSH LVLAVSSSIF ILLAAVTGSV LALEPISNRI QPYTTGDLDQ ITVAEFTHTL
QQKYAEVISV EIDKNSWVTA SVITKDGTDK IIYIDPKTGD SLGTPKETSP VFKFATTLHR
SLFLKGIGRF FVGLSSLLLC LISISGIFLI LKKQGGVKGF FKPIVKESFN PYYHTVFGKW
LLIPILIVTL TGVYLSLEQF SIIPSAKIVH QEDTLFAEEP VIPVSEFKVF KNIKLSEVRK
IEYPFAPFPE SYFLVQLTNK EYLINQFNGD IVSQVNYPFY VILTYYSTLF HTGQGSIVWS
IVLLLASIGI LFFMYSGFSI TLKRRKSRIK NKYKKDNCDY VILIGSENGN TFYFANALYS
ELLRLGKKAY LAELNSYKSY KNMQHLVVMT STYGTGEAPT NAKKFKALLN THQQGAKFNY
SVVGFGSLAY PDYCKFAYDV DTMLQAHPNN NRLADVFTIN NQSLESFNQW LLAWSKQENL
NISLPKAIGS KKKRKTYAFT VTKHTKAENN PDDTFCIYLK PVEKVKFTSG DLLSILGEKD
QRERLYSIGK WNKNELVISV KRHQKGSVSN RLQNLAVGNK ISCGIVKNKA FHLPKKAKEA
LLIATGTGIG PYLGMIHQNT AHKKLHLYWG GRTAASFELY KNQLETQQQA GNLTSLHLAL
SREQAQKVYV QNLLAANGKE VAQLIKNKGY ILICGSIGMQ KEVTTVLDTI CKNHLKKPLS
YYQNKGYILM DCY
//
