ID C6E8B3_GEOSM Unreviewed; 444 AA.
AC C6E8B3;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=Pyridine nucleotide-disulphide oxidoreductase dimerisation region {ECO:0000313|EMBL:ACT18101.1};
GN OrderedLocusNames=GM21_2049 {ECO:0000313|EMBL:ACT18101.1};
OS Geobacter sp. (strain M21).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443144 {ECO:0000313|EMBL:ACT18101.1};
RN [1] {ECO:0000313|EMBL:ACT18101.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M21 {ECO:0000313|EMBL:ACT18101.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Lovley D.;
RT "Complete sequence of Geobacter sp. M21.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR EMBL; CP001661; ACT18101.1; -; Genomic_DNA.
DR AlphaFoldDB; C6E8B3; -.
DR STRING; 443144.GM21_2049; -.
DR KEGG; gem:GM21_2049; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_3_7; -.
DR OMA; DKNHTNY; -.
DR OrthoDB; 9769238at2; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43429:SF1; NAD(P)H SULFUR OXIDOREDUCTASE (COA-DEPENDENT); 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 2..285
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 327..428
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 444 AA; 47962 MW; 02C125511F813FC6 CRC64;
MKTVIIGGVA AGLSAASQAK RLSPESEVVV LEKTGDVSYA ACGMPYNLFF KEKPVEKLYA
LSLETIRKER GIDYRLRQEV TGIDPVGKVV SVTDLATGKS YEERYDFLVY ATGNSAIRLT
APGFDDGDVF CFKTLDDTRH VKQFIYDKAP KRAVLVGAGY TNLEVADVLT NMKIKPVILE
KAPTILPSFC EEAREKVMEK VKERGVELIT GVDIAEKAGG EVRSSAGVFP ADLVVVAVGT
RPNTALFAAA GGELGTAGAA KVDRYLRTNL DSVFAGGDCA EHYVRQLGMN SYFPLGPAAN
KHGRVIGSNV SNPDHMMEFW GIDQTAVFKF FELSVATTGL NERQLLALGK DFVKVAVDNP
TRGEFPGGST MRVILFCQKG DGLLLGAQIV GEDVVAKRLD VLATAIYKQM TVFEIAELDL
AYAPPYSPVW DPILVAANVA VKKV
//