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Database: UniProt
Entry: S6AJB2_PSERE
LinkDB: S6AJB2_PSERE
Original site: S6AJB2_PSERE 
ID   S6AJB2_PSERE            Unreviewed;       367 AA.
AC   S6AJB2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Putative NADPH oxidoreductase {ECO:0000313|EMBL:BAN50862.1};
GN   ORFNames=PCA10_51300 {ECO:0000313|EMBL:BAN50862.1};
OS   Pseudomonas resinovorans NBRC 106553.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1245471 {ECO:0000313|EMBL:BAN50862.1, ECO:0000313|Proteomes:UP000015503};
RN   [1] {ECO:0000313|EMBL:BAN50862.1, ECO:0000313|Proteomes:UP000015503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 106553 {ECO:0000313|EMBL:BAN50862.1,
RC   ECO:0000313|Proteomes:UP000015503};
RX   PubMed=23887915; DOI=10.1128/genomeA.00488-13;
RA   Shintani M., Hosoyama A., Ohji S., Tsuchikane K., Takarada H., Yamazoe A.,
RA   Fujita N., Nojiri H.;
RT   "Complete Genome Sequence of the Carbazole Degrader Pseudomonas
RT   resinovorans Strain CA10 (NBRC 106553).";
RL   Genome Announc. 1:e00488-13(2013).
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DR   EMBL; AP013068; BAN50862.1; -; Genomic_DNA.
DR   RefSeq; WP_016494989.1; NC_021499.1.
DR   AlphaFoldDB; S6AJB2; -.
DR   STRING; 1245471.PCA10_51300; -.
DR   KEGG; pre:PCA10_51300; -.
DR   PATRIC; fig|1245471.3.peg.5207; -.
DR   eggNOG; COG1018; Bacteria.
DR   HOGENOM; CLU_003827_14_2_6; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000015503; Chromosome.
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; cd06216; FNR_iron_sulfur_binding_2; 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; IPR008333; Cbr1-like_FAD-bd_dom.
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; NADH OXIDOREDUCTASE HCR; 1.
DR   PANTHER; PTHR47354:SF3; OXIDOREDUCTASE; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00406; CYTB5RDTASE.
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; 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:UP000015503}.
FT   DOMAIN          46..147
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   367 AA;  39679 MW;  9EE2A2249DB511F5 CRC64;
     MYLVPLSLAR RLGPALKPLR ALVAGGWLQE ADTDCLLRLV HPALRLKRVF ARVESRVWVA
     DDMLALGLRT NGNAHGWRPG QHVRLYRELD GVRHGRSYSL TKAEPDGRIE LAVRRQPGGR
     FSNGLLERLE VGSLVELDPA QGELTWPHEA GSVLLLAAGS GITPLLGLLR HALAQGFAAP
     VTLLHYVRQR RQRAFGEELQ GLMARYPNFQ VRWAISGEAP AAGELAGRFQ AAHLAGRPVH
     SLLACGPHGF VASVDDWWRA EPRAGGLQVE AFTPPAPSVG GGEQVRLRFA RSHRELPGNS
     AVNLLEQAEA HGLRPPHGCR QGICTACTCQ LLAGGVRDLR TGGLTHGPGL PIRLCVSAPL
     GDVELDL
//
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