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Database: UniProt
Entry: R6D0L5_9FIRM
LinkDB: R6D0L5_9FIRM
Original site: R6D0L5_9FIRM 
ID   R6D0L5_9FIRM            Unreviewed;       935 AA.
AC   R6D0L5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:CDA82208.1};
GN   ORFNames=BN516_00758 {ECO:0000313|EMBL:CDA82208.1};
OS   Firmicutes bacterium CAG:176.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263007 {ECO:0000313|EMBL:CDA82208.1, ECO:0000313|Proteomes:UP000017932};
RN   [1] {ECO:0000313|EMBL:CDA82208.1, ECO:0000313|Proteomes:UP000017932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:176 {ECO:0000313|Proteomes:UP000017932};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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:CDA82208.1}.
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DR   EMBL; CBCO010000185; CDA82208.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6D0L5; -.
DR   Proteomes; UP000017932; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-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   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF00037; Fer4; 2.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 2.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017932}.
FT   DOMAIN          318..347
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          866..895
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   935 AA;  103547 MW;  DD5ED4755674F060 CRC64;
     MRDINGSKPT SFPLDEEKLS FKIPCPDRPP REKILKLGSM ITNRIGLKAT ADDPEYWGLD
     ALVTDEMADV ALKMGVRKPK TIEQLMKLTK MEREPLQKLL DEMAWLGLIE YNWENLDGKN
     PNHEKRYILP LFVPGSAEFL NMRRSQIDAH PEVAAFFERM TMLPLEKITP MVPPGGAGIG
     MHVIPVEKAI ETEQEAIGLE KISYWLHKYE GKYAKSMCSC RASRDKLGEG CGDDVENWCI
     AVGDMADYVV QTQRGEYITY DEAMAIFKQA EDNGFVHQIT NIDGEQKIFG ICNCNVNVCN
     ALRTSQMFNT PNMSRSAYVA AVETEKCVAC GRCVENCPAG AVKLGQKLCT KDGYIEYPRA
     ELPDEVKWGP EKWSVDYRDR NRINCYDTGT APCKTACPAH IAVQGYLKLA AQGKYREALQ
     LIKRENPFPA VCGRICNRRC EDACTRGTVD EAVAIDEVKR FIAQQDLDAE TRFIPEKVIP
     KVDGEFSEKI AIIGGGPAGM SCAYYLAEKG YRPTVFEKES RPGGMLMNAI PSFRLEKDVV
     EAEIDVLRAL GVEFRCGVEV GKDITIAQLR EEGYKGFYVA VGLQHGGALA VPGGDVENVI
     SGIDFIRGVH LRDEKTLKGR VVVIGGGNIA ADVARTAVRC GAESVSLYCL EGYEEMPMGE
     EDRSECEREG IAIYAGWGPK EVQTENGKAA NIAFVKCLSV KDESGRFAPV YDENTVQMAP
     CGTVLYCIGQ KAEWKTLLAG TQVEFNPNGT AKADPVTYQT AEPDIFVGGD AYTGQKFAID
     AIAAGKQGAI SLHRYVQGAT LTIGRDRRQF IELDKKNALI AVDSYDNTPR QRIGYNDALR
     KTFRDERVAF TAEQVKAETA RCLGCGASIV DPNKCIGCGV CTTKCAFDAI HLHRERPECS
     TMYACEDKMK AILPYMIKRN IKIKKAERRA KKAAK
//
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