ID A4J959_DESRM Unreviewed; 672 AA.
AC A4J959;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=FAD-dependent oxidoreductase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=Dred_3110 {ECO:0000313|EMBL:ABO51612.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO51612.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO51612.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO51612.1,
RC ECO:0000313|Proteomes:UP000001556};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000612; ABO51612.1; -; Genomic_DNA.
DR RefSeq; WP_011879401.1; NC_009253.1.
DR AlphaFoldDB; A4J959; -.
DR STRING; 349161.Dred_3110; -.
DR KEGG; drm:Dred_3110; -.
DR eggNOG; COG0644; Bacteria.
DR HOGENOM; CLU_029694_0_0_9; -.
DR OrthoDB; 9759982at2; -.
DR Proteomes; UP000001556; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR039650; HdrA-like.
DR PANTHER; PTHR43498:SF1; COB--COM HETERODISULFIDE REDUCTASE IRON-SULFUR SUBUNIT A; 1.
DR PANTHER; PTHR43498; FERREDOXIN:COB-COM HETERODISULFIDE REDUCTASE SUBUNIT A; 1.
DR Pfam; PF12831; FAD_oxidored; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001556};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 672 AA; 74170 MW; FF569095624B0637 CRC64;
MKQFKRWHYL TLGAFVVLVG FVGFLLLKGN NVNREVIPLK ANAVKASYDV VVVGGDPEGV
AAAVAAARSG RQTLLVDTRP ELGGLMTRGW LNSLDMNYGP GKEILNKGIF QEFFSQIEGD
SFDITTATNV FHQMVNREKN LDVLPGADAV LPILHGQVKP LVDPGQSVVN DKIGLAYKMK
PEQRAIVNNS AGLPQVNGVQ VRQEDKVQNI SAQRIIDATQ DGDIAAAAGV PFTYGQEDIG
NGQQGMAVTL VFKLDGISKW DWYRMMLNLN FRRFLASITG NTTEHYTGAN LHSAWGFDAI
MKGYKSNTPA VTMRGLNVGR QADNSILINA LQVFGIDGLQ AKDRKRAREL AQRELPHIVK
YMKQHIPGFG DIQLAATAPE LYVRETRHIQ GLYRLTVDDV LENRSFEDRI AYGSYPIDIQ
ATDPLFKGTV IGTPAGYAIP FRSLVPQGVD NLLVVGRAAS FDSLAHGSAR VIPVGMATGQ
AAGVAAALSL EQGISFKNLA MDKGQIQNLQ QKLTQQGVDL KELKVVSSPE TKHWAYEGLR
FMRHYGLAAG GYNNQYRLDE NMSEAHFING LHNVLKRAGI KVENKPLLST EGNALTLEDV
AYYFAQYQGL KYNKKQAYAH FTRQNFWDPR IMEEVKANRG VVTMGAGYML LQDFTEGWQD
HPPAQGTLSE RR
//
