ID U1ZVB1_9PSED Unreviewed; 682 AA.
AC U1ZVB1;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:ERI51043.1};
GN ORFNames=N878_07300 {ECO:0000313|EMBL:ERI51043.1};
OS Pseudomonas sp. EGD-AK9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1386078 {ECO:0000313|EMBL:ERI51043.1, ECO:0000313|Proteomes:UP000016488};
RN [1] {ECO:0000313|EMBL:ERI51043.1, ECO:0000313|Proteomes:UP000016488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EGD-Ak9 {ECO:0000313|Proteomes:UP000016488};
RA Kapley A., Sagarkar S., Bhardwaj P., Qureshi A., Khardenavis A.,
RA Purohit H.J.;
RT "Indian agricultural soil isolates capable of pesticide degradation.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERI51043.1}.
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DR EMBL; AVOF01000440; ERI51043.1; -; Genomic_DNA.
DR RefSeq; WP_021444996.1; NZ_AVOF01000440.1.
DR AlphaFoldDB; U1ZVB1; -.
DR PATRIC; fig|1386078.3.peg.3365; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000016488; 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; cd06184; flavohem_like_fad_nad_binding; 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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR011576; Pyridox_Oxase_put.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR PANTHER; PTHR42815; FAD-BINDING, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G07600)-RELATED; 1.
DR PANTHER; PTHR42815:SF2; FAD-BINDING, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G07600)-RELATED; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF01243; Putative_PNPOx; 1.
DR PRINTS; PR00371; FPNCR.
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; 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 331..432
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 594..682
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 682 AA; 74468 MW; 50C9CA017A86E8D4 CRC64;
MQQLPSHRHS PWHAGEKQLQ EKVGVAERME VLGQKVIRDH MPDQHRDFYR QLPFMIAGAV
DGAGQPWATL IEGEEGFVTS PDPRRLAFDL AAMALDPLDP ATSGLGAGEA IGLLGIELHT
RRRNRINGHI RQASAQRLDI DVEHSFGNCP QYIQLREYSR SPAGRGSARH DASELDARSA
AMIRGADTFF VASYVEHDDG RRSVDVSHRG GRAGFVRVEG NRLTIPDYAG NLHFNTLGNL
SVNPRAGLLF VDFATGDVLQ LAGRVEIILD SPLIQAFEGA ERLWTFDVEQ VVLRPAAASL
RWTFHEYAPT SLMTGTWAQA DARLREREQR NQWQRWRVLS LQQESSDIRS FVLAPEQGAA
PSFAAGQHLP IRISSAAGET LLRTYSLSSA PSDGVLRISV KAQGVVSRHL HEQVQVGDVL
EVRAPLGSFT LNSDTHRPLV LIGAGVGITP LLSMLREQVA LGRGRRMHFF QGARTLTDLP
FQAELRELVQ RANGLLHIHR ALSAPGSDAV LGRDYEQQGR LDLAQIKAAL AFDDHDFYLC
GPAAFTQAIY DGLRDLSVAD ARIHAEAFGP STLTRRTDGQ AATLVQPPAA SEPVPVYFTT
SAKEARWTPG SGSLLELAES RGLSPEFSCR GGSCGTCRTR LVSGQVHYPN PPAELPQDDS
VLICCAVPAQ GEGGTQPLVL DL
//
