ID A0A0S8ZA91_9PSED Unreviewed; 337 AA.
AC A0A0S8ZA91;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:KQN50299.1};
GN ORFNames=ASE98_24025 {ECO:0000313|EMBL:KQN50299.1};
OS Pseudomonas sp. Leaf48.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1736221 {ECO:0000313|EMBL:KQN50299.1, ECO:0000313|Proteomes:UP000051774};
RN [1] {ECO:0000313|EMBL:KQN50299.1, ECO:0000313|Proteomes:UP000051774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf48 {ECO:0000313|EMBL:KQN50299.1,
RC ECO:0000313|Proteomes:UP000051774};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN50299.1, ECO:0000313|Proteomes:UP000051774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf48 {ECO:0000313|EMBL:KQN50299.1,
RC ECO:0000313|Proteomes:UP000051774};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
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:KQN50299.1}.
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DR EMBL; LMLH01000014; KQN50299.1; -; Genomic_DNA.
DR RefSeq; WP_060541771.1; NZ_LMLH01000014.1.
DR AlphaFoldDB; A0A0S8ZA91; -.
DR STRING; 1736221.ASE98_24025; -.
DR OrthoDB; 9806195at2; -.
DR Proteomes; UP000051774; 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; cd06209; BenDO_FAD_NAD; 1.
DR CDD; cd00207; fer2; 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; IPR047683; BenC-like_FAD_NAD-bd.
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; IPR017938; Riboflavin_synthase-like_b-brl.
DR NCBIfam; NF040810; BenC; 1.
DR PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 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; 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 3..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 104..204
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 337 AA; 36386 MW; 19F0A7EFC9E5CE9B CRC64;
MTHSIAFSFE DGVTRFIDAH AGETVADAAY RQGINIPLDC RDGACGTCKC FAEAGRYDLG
EDYIEDALSP EEAEQGFVLT CQMRARSDCV VRVPASSDVC RTRQASYDAT ISAVRQLSDS
TIALSIKGDA LGKLAFLPGQ YVNLGIPGSE QTRAYSFSSL QRDGEVSFLI RNVPGGLMSS
FLTGMAKVGD SINLAGPLGS FYLRDIRRPL LLLAGGTGLA PFTAMLEKIA EQGSEHPLHL
IYGVTHDFDL VQLDRLEAFA ARIPNFSFSA CVASPESRHP LKGYVTQHIE PGHLHDGDVD
VYLCGPPPMV EAVSQFIREQ GIAPANFYYE KFAASAA
//
