ID A0A1H7L5J1_9BURK Unreviewed; 549 AA.
AC A0A1H7L5J1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Ferredoxin-NADP reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SAMN05216359_10435 {ECO:0000313|EMBL:SEK93527.1};
OS Roseateles sp. YR242.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1855305 {ECO:0000313|EMBL:SEK93527.1, ECO:0000313|Proteomes:UP000198631};
RN [1] {ECO:0000313|EMBL:SEK93527.1, ECO:0000313|Proteomes:UP000198631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR242 {ECO:0000313|EMBL:SEK93527.1,
RC ECO:0000313|Proteomes:UP000198631};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOAV01000004; SEK93527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7L5J1; -.
DR STRING; 1855305.SAMN05216359_10435; -.
DR OrthoDB; 370747at2; -.
DR Proteomes; UP000198631; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06185; PDR_like; 1.
DR Gene3D; 3.10.20.30; -; 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; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR011576; Pyridox_Oxase_put.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01243; Putative_PNPOx; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF50475; FMN-binding split barrel; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714}.
FT DOMAIN 231..337
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 462..549
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 549 AA; 59347 MW; 1629F802B527D94F CRC64;
MGRAYSDITF TPGVREVQAE LGSREQYAFL DTMADRGDSL TPREIQFIEQ ADHFFQATVS
ETGWPYVQHR GGPKGFLKVI NPKVIGFADF RGNLQYLSVG NLRRDDRISL ILVDFPNQRR
LKLLGRVQLV EAGESKEADA AIAAVANPAY AATVERAFLI AIEGWDWNCP QHITPRFTET
EVVHLMTPLR AQVQKLKAQL EEARSVTLAV PPAPSAPSPP SSPAGSLALG DGPLSLTVVG
VRQLTKAVRA YELVSTDGGQ LPAVQAGAHL DVPMRLANGV LTTRSYSIAS SPLRRDAFEI
AVLHEAAGTG GSAAVHETFA IGTRIRCAMP ENNFPLAPQP HRAILVAGGI GITPLKAMAH
ALAASGRDFE LHFACRSQAQ APFLGQLIEQ FGHRVIVHSA QDGQRLDVAG LLKSLGDSDH
LYVCGPPRLI DAVRLGAAEL GMAADRVHVE RFTLPQDKAG DRAFDVHLDK SGRTIQVPPQ
RSILEALEAQ GLHPPASCRI GTCGTCATRV VDGVPLHRDD VLTPDQREKQ HLMCICVSRS
ESDELHLSL
//
