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Database: UniProt
Entry: A0A1I2ZS22_9RHOB
LinkDB: A0A1I2ZS22_9RHOB
Original site: A0A1I2ZS22_9RHOB 
ID   A0A1I2ZS22_9RHOB        Unreviewed;       327 AA.
AC   A0A1I2ZS22;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Ferredoxin-NADP reductase {ECO:0000313|EMBL:SFH40554.1};
GN   ORFNames=SAMN04488021_11053 {ECO:0000313|EMBL:SFH40554.1};
OS   Paracoccus aminovorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=34004 {ECO:0000313|EMBL:SFH40554.1, ECO:0000313|Proteomes:UP000183635};
RN   [1] {ECO:0000313|EMBL:SFH40554.1, ECO:0000313|Proteomes:UP000183635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8537 {ECO:0000313|EMBL:SFH40554.1,
RC   ECO:0000313|Proteomes:UP000183635};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOPU01000010; SFH40554.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2ZS22; -.
DR   STRING; 34004.SAMN04488021_11053; -.
DR   Proteomes; UP000183635; 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; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00410; PHEHYDRXLASE.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183635}.
FT   DOMAIN          5..113
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          242..327
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   327 AA;  34729 MW;  85F390622E02A2B5 CRC64;
     MMGGAGHIPA RVLRREPAGE GVLRLVLAPV GAPGFPAWQP GAHADLVLPG GDAAGEPLVR
     QYSLCGDPAD LSEYHFGILR EADGRGGSTW VHDRLRVGDE IAVGAPRNHF PFAPVAAPAA
     RTLFIAGGIG ITPILPMLRQ AMAEDRDWRL VAAARSRARL PFRAELAALP AHRLRLHCDD
     EAGLLDLAGL LAGEGAGTTV YSCGPAPLLD ALQSLAEDAP WQLRIERFSA QPAPAGRSDR
     PFEVVCRASG KRLRVPADKS VLQVLREAGL RVESSCRDGV CGTCELRVLA GTPDHRDSVL
     TAEERAEGTH MMVCVSRAVG DVLELDI
//
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