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Database: UniProt
Entry: E3FHD2_STIAD
LinkDB: E3FHD2_STIAD
Original site: E3FHD2_STIAD 
ID   E3FHD2_STIAD            Unreviewed;       425 AA.
AC   E3FHD2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=FAD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:ADO75348.1};
GN   OrderedLocusNames=STAUR_7593 {ECO:0000313|EMBL:ADO75348.1};
OS   Stigmatella aurantiaca (strain DW4/3-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO75348.1, ECO:0000313|Proteomes:UP000001351};
RN   [1] {ECO:0000313|EMBL:ADO75348.1, ECO:0000313|Proteomes:UP000001351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO75348.1,
RC   ECO:0000313|Proteomes:UP000001351};
RX   PubMed=21037205; DOI=10.1093/molbev/msq292;
RA   Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA   Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA   Sogaard-Andersen L.;
RT   "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL   Mol. Biol. Evol. 28:1083-1097(2011).
CC   -!- SIMILARITY: Belongs to the NADH dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00005272}.
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DR   EMBL; CP002271; ADO75348.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3FHD2; -.
DR   STRING; 378806.STAUR_7593; -.
DR   KEGG; sur:STAUR_7593; -.
DR   eggNOG; COG1252; Bacteria.
DR   HOGENOM; CLU_021377_8_0_7; -.
DR   Proteomes; UP000001351; Chromosome.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006116; P:NADH oxidation; IEA:InterPro.
DR   Gene3D; 3.50.50.100; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR045024; NDH-2.
DR   PANTHER; PTHR43706; NADH DEHYDROGENASE; 1.
DR   PANTHER; PTHR43706:SF45; NADH DEHYDROGENASE-LIKE PROTEIN RV1812C; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          27..337
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   425 AA;  45619 MW;  16459E56D4FA2823 CRC64;
     MHPHGGTMLR VRRLNDNPTE SKTMTQKIVI AGSGFAGMWA AISAARAVSL AGKENEVEIT
     IVSPSPHLHI RPRLYETVFE EMAPDLAPLF KAIGVRHLAG TVEAIHAGSH QVEVLGADGQ
     RTTLPYDRFV LAAGSRLFMP NVPGLKEHAF NVDQLSSAMA LDAHLKALAH KPETAARNTV
     VVAGGGFTGI ETATEMPQRL RAIFGQDAKI RVVVVEQAPV IGPDLGPVPR PIIEEALAEC
     GVEVRTSTGA TAIDAKGVTL STGERIDTQT VVWTAGSRAN PLAAQIEGEH DRFGRVHADP
     YLRAKSVKDI FVTGDVALAA TDDQGNVASM SCQHAIRLGR FAGHNAAAEL VGLPVQPYRQ
     PRYVTCLDLG AWGAIFTEGW DRQVRLKRAE GKATKREINT KWIYPPQADR DAAFALANLD
     DAVVA
//
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