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Database: UniProt
Entry: A0A086D183_9GAMM
LinkDB: A0A086D183_9GAMM
Original site: A0A086D183_9GAMM 
ID   A0A086D183_9GAMM        Unreviewed;       357 AA.
AC   A0A086D183;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=NADH oxidase {ECO:0000313|EMBL:KFF48197.1};
GN   ORFNames=GY26_15705 {ECO:0000313|EMBL:KFF48197.1};
OS   Gammaproteobacteria bacterium MFB021.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1492922 {ECO:0000313|EMBL:KFF48197.1, ECO:0000313|Proteomes:UP000028732};
RN   [1] {ECO:0000313|EMBL:KFF48197.1, ECO:0000313|Proteomes:UP000028732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MFB021 {ECO:0000313|EMBL:KFF48197.1,
RC   ECO:0000313|Proteomes:UP000028732};
RA   Joseph T.C., Baby A., Varghese A.M., Reghunathan D., Murugadas V.,
RA   Lalitha K.V.;
RT   "Draft Genome sequence of a halophilic and highly halotolerant unknown
RT   Gammaproteobacteria strain MFB021.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KFF48197.1}.
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DR   EMBL; JNVT01000100; KFF48197.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A086D183; -.
DR   STRING; 1492922.GY26_15705; -.
DR   eggNOG; COG1018; Bacteria.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000028732; 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; cd06215; FNR_iron_sulfur_binding_1; 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:SF6; 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; 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          11..117
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          273..357
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   357 AA;  38849 MW;  45857F4CF36B4AB9 CRC64;
     MGALASGTPP TFWHDSEILE CVSVLPEAPN VATFCFQAPS GGLFSFLPGQ FLTLELPTAE
     GIVHRTYTIS SSPSRPMSLT ITVKAQSDSI GTRWMLDHLQ PGMRVKAIGP GGRFSLDDAP
     ARKYLFISAG SGITPMMSMT TYLYDQGRDP DIVFVNCARR PSEIIFRERL EHIASRVTGI
     ELRWVVEQTD RYTPWTGYQG FFNQLMLGLM APDYLEREVF CCGPEPFMQA VRDALVGLGF
     DLENHYHQES FDAPLPETSD VPDSVVLDEE SRAEIAFSRS AVTHRCSETE TLLGAAKAAG
     VLIPSGCTFG VCGSCKVKKL AGDVHMVHNG GITDADIEAG YVLACCSHPR GAVVIDA
//
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