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Database: UniProt
Entry: A0A1F4I157_9BURK
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ID   A0A1F4I157_9BURK        Unreviewed;      1074 AA.
AC   A0A1F4I157;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=NAD-binding oxidoreductase {ECO:0000313|EMBL:OGB03871.1};
GN   ORFNames=A3E25_09135 {ECO:0000313|EMBL:OGB03871.1};
OS   Burkholderiales bacterium RIFCSPHIGHO2_12_FULL_69_20.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=1797561 {ECO:0000313|EMBL:OGB03871.1, ECO:0000313|Proteomes:UP000177017};
RN   [1] {ECO:0000313|EMBL:OGB03871.1, ECO:0000313|Proteomes:UP000177017}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGB03871.1}.
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DR   EMBL; MESD01000048; OGB03871.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F4I157; -.
DR   Proteomes; UP000177017; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; 3.30.70.20; -; 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; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR028894; RDH_dom.
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; PF13486; Dehalogenase; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   PRINTS; PR00409; PHDIOXRDTASE.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 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; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          545..575
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          752..857
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          986..1074
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   1074 AA;  117406 MW;  5C7BEEE94E29F998 CRC64;
     MRFFSYQDRP VHLGPYPLER LTRTADAPDL QAVPALQPVD FDAPDALSIA HAMKRYIGMF
     DVVRDGAVAA LPAEAPTDPT ERAQHLKAAG YYFDASMMGI CQLSAAALRA QPLRNPAVAG
     IADELARSQP QSFAAGMDMI LADVLESART LHGPIDHHTH AIVIAVEFQR DPRPGEPGSD
     WIAGTQAQRA AVLAAQTAVL LSTYLRLLGF EARAHSATCS EVDLNRLAVA AGLAHADLSH
     PYLGTRFGLA AVSTTFQMAV DEALAPPAQQ DRRRSHGLAW QLGMGTLKSA IHQDPYARRD
     FRLGPHPFET LQRRDEPTTF IDHARVPRFP KRADFFARAL FGDLGRDVQA SAKNAHYVMK
     SPIGACARRA LGALLLLQFG EARGPVSPTV ADPQRNADNL KATAYYLGCD AVGLCAVPEW
     AYYSHDAGGN ALPAYHANGI NLLLDQGHET MEGASGDDWI SVAQSMRAYL RFSLLGGIVA
     EQVRRLGYSA RVHSVLDGDV LQPPLLLLSG LGEVSRIGEV ILNPYLGPRL KSGTVTTDLP
     MVMDRPIDFG LQRFCEQCNK CARECPSGAI TAGPKRMYNG YEIYKSDAEK CARYRITNAG
     GGMCGRCMKT CPWNLEGLFA DSAFRWLAMH LPGQARHLAA LDDHWGRGRI NPVKTWWWDL
     ELDRGTQRYV QAKLTHRREL NIGLKIDPAL QSLAVYPADQ MPPPYPVAFP VDREQGIARY
     RALLSPAQYR EKLARGDTAD LAPPFQLPAG EPPVFPVLLQ RREDMAPDVA KYEFVARDGG
     QLPPFEAGAH IDVVIAPEYL RPYSLAGDPA DRSKWVLGVQ REAPEHGGRG GSALMHRAFR
     AGRMVFVSKP NNLFKLHEEA TMSWLFAGGI GVTPLLTMAH RLHAIGKPFE LHYSAASRGT
     AGFVADIEAA AWHAQAHCHF KDEGRRADLP RLIPPHTPGA HLYTCGSARY MDSIFDTARA
     AGWPDEALHR EFFSVPEAPP RENHAFTLRL LASGRTLEVP AERCATEVLA AAGLKVDVKC
     SDGLCGVCAL AYDPAASDQI DHRDVVLSTA ERRERVILCC ARTVQPGGVI ALRL
//
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