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Database: UniProt
Entry: C6E8B3_GEOSM
LinkDB: C6E8B3_GEOSM
Original site: C6E8B3_GEOSM 
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
//
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