ID A0A1Y1I675_KLENI Unreviewed; 1300 AA.
AC A0A1Y1I675;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=NADPH--hemoprotein reductase {ECO:0000256|ARBA:ARBA00023797};
DE EC=1.6.2.4 {ECO:0000256|ARBA:ARBA00023797};
GN ORFNames=KFL_002120130 {ECO:0000313|EMBL:GAQ84919.1};
OS Klebsormidium nitens (Green alga) (Ulothrix nitens).
OC Eukaryota; Viridiplantae; Streptophyta; Klebsormidiophyceae;
OC Klebsormidiales; Klebsormidiaceae; Klebsormidium.
OX NCBI_TaxID=105231 {ECO:0000313|EMBL:GAQ84919.1, ECO:0000313|Proteomes:UP000054558};
RN [1] {ECO:0000313|EMBL:GAQ84919.1, ECO:0000313|Proteomes:UP000054558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2285 {ECO:0000313|EMBL:GAQ84919.1,
RC ECO:0000313|Proteomes:UP000054558};
RX PubMed=24865297; DOI=10.1038/ncomms4978;
RA Hori K., Maruyama F., Fujisawa T., Togashi T., Yamamoto N., Seo M.,
RA Sato S., Yamada T., Mori H., Tajima N., Moriyama T., Ikeuchi M.,
RA Watanabe M., Wada H., Kobayashi K., Saito M., Masuda T.,
RA Sasaki-Sekimoto Y., Mashiguchi K., Awai K., Shimojima M., Masuda S.,
RA Iwai M., Nobusawa T., Narise T., Kondo S., Saito H., Sato R., Murakawa M.,
RA Ihara Y., Oshima-Yamada Y., Ohtaka K., Satoh M., Sonobe K., Ishii M.,
RA Ohtani R., Kanamori-Sato M., Honoki R., Miyazaki D., Mochizuki H.,
RA Umetsu J., Higashi K., Shibata D., Kamiya Y., Sato N., Nakamura Y.,
RA Tabata S., Ida S., Kurokawa K., Ohta H.;
RT "Klebsormidium flaccidum genome reveals primary factors for plant
RT terrestrial adaptation.";
RL Nat. Commun. 5:3978-3978(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:60344; EC=1.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036596};
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 -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC family. {ECO:0000256|ARBA:ARBA00010018}.
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DR EMBL; DF237161; GAQ84919.1; -; Genomic_DNA.
DR STRING; 105231.A0A1Y1I675; -.
DR OrthoDB; 276396at2759; -.
DR Proteomes; UP000054558; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR CDD; cd00302; cytochrome_P450; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
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:SF17; NADPH--CYTOCHROME P450 REDUCTASE; 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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF48264; Cytochrome P450; 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 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Membrane {ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054558};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 617..763
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 856..1099
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 784..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..824
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1300 AA; 143385 MW; 84F494F1807E8793 CRC64;
MLNGAAAAMN GTVTMELLSE TVERLPLAEL AFYPVAFMVL LLSWTTRAAT PDPAAMAYKL
GLPFLGRLAP SLNMGSLLVF VAVYFGSSMG NWALAWVAVV LAAVTCPKPI EMVLLNAIVK
SSLFGSSRKV ETFMVDLLRI ARELAAKQGQ PKDALIDCLK FELPFMLPIY VLIDVHYAHF
LHAAPTCEFF ATDYKARDWF IGPNLLTAKS PPMKNPEWLM HRALTAAVNV DRNGIESTMG
RMVVQGMKIL AEMSRDLKKK YGSVIDLCEE FEHIIVTAHL SAMFGQAYTD KFPMISKEVN
YTAIKYSSVS NGMQIKVWQP LEGLKFLDGR KKVVDSLLWA LEHSDSALLE IIRKAHKEGK
ITHEELLGTC LLFTYALAPS RTSIFGLSLL ANLPHEQDRV AKEVRTTLPD VFDEKTGEFD
PKKVDVWMTE LDECDNLKRA VRETLRLYPG VPMFIPQMAA RDVQIGPWQI PKGALTMSMP
FLSQRDGKVH QNPDQFDPTR NLEKGAPLPD GTLTYFPFAM GPRSCQGQFY GELLVRAAMG
IALRDHEFEA KGPVPPPAML GFIHPMTPAW AKIQPPPVEQ KKKTEVAKAV PAAAGKPQLS
AMNSIKEVPR LSNVDTITVL YASTQGTSRA FADRLARGLQ ESDLSELADT PAIKVFDAAD
YSMQQLTRES LVIFVTSTFG HNQPPYSGSN LKAFVNKPDT KLPNLAYAVL ALGNSVYPSF
CSFGKLFDKR LAEVGAQRLM PVTLCDEIEG QEGAFNAFLE QIADVLYSAL GGGDGAPSPV
SVLPVTRSST GKGKPPAGAP AAGPPMVKKH KSADPKRVES AQHHKRFELV ELGRGQIARQ
RPAGPIKEGA PKGTRDHPVE LQVIANRCLR PYTSLAQIRN VVVRTPSDGS LTYQPGDLLG
VYPVNRLDLV TSLSERLGIT DLDTEFELRP LRGKDQLASP LPDKMTYWLA LTSYLAIQRV
PQPQLLKVLQ QYTTDPEEAS WLGQLGAGGP KYTEFAMGSH SLLETLYRVP SCKPDVAHLF
ETLPHLQPRM YSISSSPLYH RGQAHLTIAE LIYQSHDASW KRGVCSTFLG TDIMIPSSMA
DPNCRLLGYV MPNPGFHLPE SASTPIVMIG IGSGIAPFRG FWQHRLAMLK DSKNTTQLGD
ALLYAGFQSK VNSCYLDELE QAQKEGALSK ARVVYSREGE RKYVTHALTE DRWSLWHEYL
SQGAVVYVCG TINAANDVRE TILGVMKEAG GMSEEDAEAW LESARDRDQY KEDVFGESTA
SYSKTRMQAR LRSAKVKLRS SFHFLGAKGI AKILESAPPM
//
