ID D8GSW9_CLOLD Unreviewed; 626 AA.
AC D8GSW9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:ADK14539.1};
DE EC=1.6.99.5 {ECO:0000313|EMBL:ADK14539.1};
GN OrderedLocusNames=CLJU_c14710 {ECO:0000313|EMBL:ADK14539.1};
OS Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=748727 {ECO:0000313|EMBL:ADK14539.1};
RN [1] {ECO:0000313|EMBL:ADK14539.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 13528 {ECO:0000313|EMBL:ADK14539.1};
RA Koepke M., Hujer S., Held C., Wiezer A., Liesegang H., Ehrenreich A.,
RA Gottschalk G., Duerre P.;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADK14539.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13528 {ECO:0000313|EMBL:ADK14539.1};
RX PubMed=20616070; DOI=10.1073/pnas.1004716107;
RA Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A.,
RA Ehrenreich A., Liebl W., Gottschalk G., Durre P.;
RT "Clostridium ljungdahlii represents a microbial production platform based
RT on syngas.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010).
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
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DR EMBL; CP001666; ADK14539.1; -; Genomic_DNA.
DR RefSeq; WP_013238136.1; NZ_LITS01000006.1.
DR AlphaFoldDB; D8GSW9; -.
DR STRING; 748727.CLJU_c14710; -.
DR KEGG; clj:CLJU_c14710; -.
DR PATRIC; fig|748727.19.peg.2954; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_3_2_9; -.
DR OrthoDB; 9761899at2; -.
DR Proteomes; UP000001656; 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; 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.
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:ADK14539.1};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 569..598
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 599..626
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 626 AA; 68172 MW; 3F67A303CD700A08 CRC64;
MDKIKSFEDL KALREKYKAK IANRTYDNAD KNIKKTLLVC GGTGCRASRS LDIVNILKTE
IKNAGLENTV DVISTGCFGF CEKGPIVKVV PDNVFYVEVN TERAKLIVYE HMAKNTVVDE
ALYRDPITKE KISKQTDIPF YKNQERIALR NCGLLNPEDI TEYIAMNGYE ALGRVLTQMT
PDSTIDEIKK SGLRGRGGGG FPTGVKWEMT RKSKSDTKFM ICNADEGDPG AFMDRSILEG
DPNSVLEAMA IAGYCIGANK GYIYIRAEYP LAINRLKIAL KQAYNLGLLG DNILGTNFSF
HIDLKYGAGA FICGEETALI NSIEGGRGEP TVKPPFPSQI GLWKKPTNIN NVETLANIPP
IILKGSKWFS SIGTEKSKGT KVFALAGKIN NVGLVEVPMG ITLREIIYNL GGGIRGGKKF
KAVQTGGPSG GCIPADHLDT AIDYESLTEI GSMMGSGGMI VMDEDNCMVN IAKFYLQFSV
DESCGKCTAC RIGNKRLLEI LEDITKGKGT MEHLEGLKDL SYVIKDSALC GLGQTSPNPI
ISTMKFFWDE YVAHVKDKRC PAGVCTALLK YNINSEKCIG CTACTKVCPK GAISGEIKKS
HVIDKSKCIN CGACSSTCKF SAITKE
//
