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Database: UniProt
Entry: D7CIW6_SYNLT
LinkDB: D7CIW6_SYNLT
Original site: D7CIW6_SYNLT 
ID   D7CIW6_SYNLT            Unreviewed;       605 AA.
AC   D7CIW6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:ADI02844.1};
DE            EC=1.6.99.5 {ECO:0000313|EMBL:ADI02844.1};
GN   OrderedLocusNames=Slip_2098 {ECO:0000313|EMBL:ADI02844.1};
OS   Syntrophothermus lipocalidus (strain DSM 12680 / TGB-C1).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophothermus.
OX   NCBI_TaxID=643648 {ECO:0000313|EMBL:ADI02844.1, ECO:0000313|Proteomes:UP000000378};
RN   [1] {ECO:0000313|Proteomes:UP000000378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378};
RX   DOI=10.4056/sigs.1233249;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Djao O., Zhang X., Lucas S., Lapidus A., Glavina Del Rio T., Nolan M.,
RA   Tice H., Cheng J., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA   Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.,
RA   Jeffries C., Rohde M., Sikorski J., Spring S., Goker M., Detter J.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA   Klenk H.;
RT   "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB-
RT   C1T).";
RL   Stand. Genomic Sci. 3:267-275(2010).
RN   [2] {ECO:0000313|EMBL:ADI02844.1, ECO:0000313|Proteomes:UP000000378}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12680 / TGB-C1 {ECO:0000313|Proteomes:UP000000378};
RX   PubMed=21304731;
RA   Djao O.D., Zhang X., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA   Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA   Brambilla E., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Rohde M., Sikorski J., Spring S., Goker M., Detter J.C.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Syntrophothermus lipocalidus type strain (TGB-
RT   C1).";
RL   Stand. Genomic Sci. 3:268-275(2010).
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00007523}.
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DR   EMBL; CP002048; ADI02844.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7CIW6; -.
DR   STRING; 643648.Slip_2098; -.
DR   KEGG; slp:Slip_2098; -.
DR   eggNOG; COG1894; Bacteria.
DR   HOGENOM; CLU_014881_3_2_9; -.
DR   Proteomes; UP000000378; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   CDD; cd02980; TRX_Fd_family; 1.
DR   Gene3D; 3.10.20.600; -; 1.
DR   Gene3D; 3.30.70.20; -; 2.
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; IPR001949; NADH-UbQ_OxRdtase_51kDa_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; PF01257; 2Fe-2S_thioredx; 1.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF13237; Fer4_10; 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; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 1.
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:ADI02844.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000378};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          548..577
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          578..605
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   605 AA;  65568 MW;  F1FA7EFAD5056ABE CRC64;
     MDQRAMLEPN IRTVLVCCGT GCLANGSMDV FRALQKQLET EGGEFQVRTY TKATGCNGWC
     EKGPLVKIVP DDITYCNVKA SDVPAIVDKT LKKGEVVKKL LYRDPKTKKY FKSHREISFY
     TKQLKVALRN IGEIDPANIQ DYIARDGYQA LAKVLKSMSP EQVIDEVQRS GLRGRGGAGF
     PTGLKWKACA SQAAEPRYVV CNGDEGDPGA FMDRSIMEGD PHSVIEGMII GAYAVGAAAG
     FIYVRDEYDL AVVNLGRAIE DARRSGYLGD NILGSGFSFD IEIVRGGGAF VCGEETALLA
     SIEGNVGEPR DKYVYPTEKG LWGQPTVINN VESWANVPVI INRGADEWAR VGTATSKGTK
     VFSLVGKVYN TGLVEVPMGT TLREIIFDIG GGIPNGRQFK AVQTGGPSGG CIPASLIDLP
     VDFDSLTSVG SMMGSGGMIV MDDRTCMVEV ARYYLNFLAG ESCGKCVPCR EGIRRMLEIL
     TRICNAQGHP EDLEILSSLG ETLQVASLCG LGKTAPNPVL STLRYFRDEY VAHIVEKRCP
     AGVCRSMTEF YIDASLCTGC GLCKKNCPAD AISGEIKEVH VIDQDRCIKC GECINNCKFQ
     AVKVR
//
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