ID Q0AZ70_SYNWW Unreviewed; 590 AA.
AC Q0AZ70;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:ABI67984.1};
DE EC=1.6.99.5 {ECO:0000313|EMBL:ABI67984.1};
GN OrderedLocusNames=Swol_0657 {ECO:0000313|EMBL:ABI67984.1};
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI67984.1, ECO:0000313|Proteomes:UP000001968};
RN [1] {ECO:0000313|Proteomes:UP000001968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968};
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
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DR EMBL; CP000448; ABI67984.1; -; Genomic_DNA.
DR RefSeq; WP_011640089.1; NC_008346.1.
DR AlphaFoldDB; Q0AZ70; -.
DR STRING; 335541.Swol_0657; -.
DR KEGG; swo:Swol_0657; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_3_2_9; -.
DR OrthoDB; 9761899at2; -.
DR Proteomes; UP000001968; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 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:UniProtKB-KW.
DR CDD; cd02980; TRX_Fd_family; 1.
DR Gene3D; 3.10.20.600; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 6.10.250.1450; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR PANTHER; PTHR43578:SF3; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF10531; SLBB; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF142019; Nqo1 FMN-binding domain-like; 1.
DR SUPFAM; SSF142984; Nqo1 middle domain-like; 1.
DR SUPFAM; SSF140490; Nqo1C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:ABI67984.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001968};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 528..557
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 559..590
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 590 AA; 63805 MW; 0705B403002ABFA2 CRC64;
MKVRLGLGSC GIAAGGLQVL EALQKEMESR GIKLEIQKSG CIGLCHHEPL LDWIEDDGRV
FTYGAVDAGR SVEILEAHLA GCGPLEAYLV SSSDEPAEFL QQQLRIVLRN CGRIDPESID
DYRRQDGYSA LQKVLAKMSP EEVIEEIEVS ALRGRGGAGF LTGLKWKATR EAGGLYRYII
CNADEGDPGA FMDRSILEGD PHAVLEGMII AAYAIGAEQG IIYCRAEYPL AVKRLEIAIA
QARQKGLLGQ RILGSDFSFD ISIQQGAGAF VCGEETALIA SLEGERGMPR LKPPYPSESG
LWGYPSSINN VETLANVPWI IRNGGEAFAA LGSRESKGTK VFALAGKIER GGLVEVPMGT
TLREIIYGIG GGVKTGRRIK AVQMGGPSGG CIPAELLDIP VDYQSLSNTG AIMGSGGMVV
LDESSCMVDL ARFFLDFTQK ESCGKCVQCR IGTKRMLEIL ERICQGEGQE GDIELLEELS
AHISENSLCG LGQSAPNPVL TTIRYFRDEY EAHIREKKCP AKQCQELLQY IIDPDRCMGC
GLCVYACPAD CIKGGENNQP YYIEQENCSK CGACLDICPE RFAAVRVPGT
//
