ID R4YT84_OLEAN Unreviewed; 388 AA.
AC R4YT84;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Oxidoreductase FAD-binding domain protein {ECO:0000313|EMBL:CCK75559.1};
GN ORFNames=OLEAN_C13830 {ECO:0000313|EMBL:CCK75559.1};
OS Oleispira antarctica RB-8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Oleispira.
OX NCBI_TaxID=698738 {ECO:0000313|EMBL:CCK75559.1, ECO:0000313|Proteomes:UP000032749};
RN [1] {ECO:0000313|EMBL:CCK75559.1, ECO:0000313|Proteomes:UP000032749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23877221; DOI=10.1038/ncomms3156;
RA Kube M., Chernikova T.N., Al-Ramahi Y., Beloqui A., Lopez-Cortez N.,
RA Guazzaroni M.E., Heipieper H.J., Klages S., Kotsyurbenko O.R., Langer I.,
RA Nechitaylo T.Y., Lunsdorf H., Fernandez M., Juarez S., Ciordia S.,
RA Singer A., Kagan O., Egorova O., Petit P.A., Stogios P., Kim Y.,
RA Tchigvintsev A., Flick R., Denaro R., Genovese M., Albar J.P., Reva O.N.,
RA Martinez-Gomariz M., Tran H., Ferrer M., Savchenko A., Yakunin A.F.,
RA Yakimov M.M., Golyshina O.V., Reinhardt R., Golyshin P.N.;
RT "Genome sequence and functional genomic analysis of the oil-degrading
RT bacterium Oleispira antarctica.";
RL Nat. Commun. 4:2156-2156(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FO203512; CCK75559.1; -; Genomic_DNA.
DR AlphaFoldDB; R4YT84; -.
DR STRING; 698738.OLEAN_C13830; -.
DR KEGG; oai:OLEAN_C13830; -.
DR PATRIC; fig|698738.3.peg.1433; -.
DR HOGENOM; CLU_003827_14_4_6; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000032749; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000032749}.
FT DOMAIN 55..155
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 308..388
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 388 AA; 43322 MW; AE15A09F99982208 CRC64;
MLNKLFSQPL GKAVTRVLEV FHPWLFKTLG RDRLEYIASN TTNELTQKID PFIWTYACKA
KVISIRQETV NTKTFVLLPN QNFKAPIAGQ HIELTSIGAN KQASRCYTLS EITPNTVSIT
VKLNPEGEVS PWLHNQAEVG TVFDISLPRG NFVHRNQDKL LFICAGSGIT PAFSMINNLL
NCSNKAGEAN KATPQVGLFY RTQTPENTIF SRRLVQLQAN HDNIKIELSY SRLPVDIVTP
SYIDQLMSAY PDIKQQHIYL CGPELFRNDV IQYLESIDFD FDHLDVEQFT LPVIEGSQGG
NDNAVLEGDV TVILKSQNIN FVIPARDCHK TLLEAAEEQG IVMEHGCRSG MCGSCKTNLV
SGEVRGNKIG RSIYPCTAYP ASKQIVLQ
//
