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Database: UniProt
Entry: A0A075JF62_9MICO
LinkDB: A0A075JF62_9MICO
Original site: A0A075JF62_9MICO 
ID   A0A075JF62_9MICO        Unreviewed;       343 AA.
AC   A0A075JF62;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Ferredoxin {ECO:0000313|EMBL:AIF39887.1};
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:TJZ97996.1};
GN   ORFNames=FA951_02085 {ECO:0000313|EMBL:TJZ97996.1}, HX89_01600
GN   {ECO:0000313|EMBL:AIF39887.1};
OS   Dermacoccus nishinomiyaensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Dermacoccus.
OX   NCBI_TaxID=1274 {ECO:0000313|EMBL:AIF39887.1, ECO:0000313|Proteomes:UP000027986};
RN   [1] {ECO:0000313|EMBL:AIF39887.1, ECO:0000313|Proteomes:UP000027986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M25 {ECO:0000313|EMBL:AIF39887.1,
RC   ECO:0000313|Proteomes:UP000027986};
RA   Hong K.W., Chan K.G.;
RT   "Genome Sequencing of Dermacoccus nishinomiyaensis.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TJZ97996.1, ECO:0000313|Proteomes:UP000307824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSA37 {ECO:0000313|EMBL:TJZ97996.1,
RC   ECO:0000313|Proteomes:UP000307824};
RA   Williams A.N., Maclea K.S.;
RT   "Genome sequence of Dermacoccus nishinomiyaensis strain TSA37.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP008889; AIF39887.1; -; Genomic_DNA.
DR   EMBL; SUPQ01000002; TJZ97996.1; -; Genomic_DNA.
DR   RefSeq; WP_038566511.1; NZ_VEFV01000001.1.
DR   AlphaFoldDB; A0A075JF62; -.
DR   STRING; 1274.HX89_01600; -.
DR   GeneID; 41839940; -.
DR   KEGG; dni:HX89_01600; -.
DR   eggNOG; COG1018; Bacteria.
DR   HOGENOM; CLU_003827_17_0_11; -.
DR   OrthoDB; 502624at2; -.
DR   Proteomes; UP000027986; Chromosome.
DR   Proteomes; UP000307824; 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   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:UP000027986}.
FT   DOMAIN          6..132
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          256..343
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   343 AA;  37123 MW;  9E696A13EC750087 CRC64;
     MVSESTQPEA KTLLVVDGID DAADGVRLLT LRAADGADLP EWAPGAHLDL VLGGVSDAEL
     KDAEQGDLPE HDPFDELIRQ YSLCGDPADR SRFQVAVLRE SESRGGSSYI HETLKVGDEL
     VSYGPRNHFE LRKAPTYVFV AGGIGITPIL TMVRAAQAQG KNWHLYYLGR SGATMAFRDE
     LASFGDRVTF WPKADKGAFD LAATLDDADA AGPALVYSCG PERLLAAIED GCKSRANLVA
     HVERFSPKEI DDSGNTEFDV ILEESDMRLT VPADRSIFEV VREAGVSVLG SCLEGICGTC
     ETGVIAGEID HRDSVLEDDE REEGDIMMIC VSRCKGKELT LEL
//
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