ID C6PY42_9CLOT Unreviewed; 631 AA.
AC C6PY42;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:EET85830.1};
DE EC=1.6.99.5 {ECO:0000313|EMBL:EET85830.1};
GN ORFNames=CcarbDRAFT_3709 {ECO:0000313|EMBL:EET85830.1};
OS Clostridium carboxidivorans P7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536227 {ECO:0000313|EMBL:EET85830.1, ECO:0000313|Proteomes:UP000004198};
RN [1] {ECO:0000313|EMBL:EET85830.1, ECO:0000313|Proteomes:UP000004198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P7 {ECO:0000313|EMBL:EET85830.1,
RC ECO:0000313|Proteomes:UP000004198};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Hemme C.L.;
RT "The draft genome of Clostridium carboxidivorans P7.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EET85830.1}.
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DR EMBL; ACVI01000074; EET85830.1; -; Genomic_DNA.
DR RefSeq; WP_007062594.1; NZ_GG770685.1.
DR AlphaFoldDB; C6PY42; -.
DR STRING; 536227.Ccar_10130; -.
DR KEGG; cck:Ccar_10130; -.
DR PATRIC; fig|536227.13.peg.2119; -.
DR eggNOG; COG1894; Bacteria.
DR OrthoDB; 9761899at2; -.
DR Proteomes; UP000004198; Unassembled WGS sequence.
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; -; 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; 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; PF00037; Fer4; 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:EET85830.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004198};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 575..603
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 604..631
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 631 AA; 68301 MW; E826552F97F18465 CRC64;
MNKINSYEEL QKACLKYSEN LKIRESSEEE EAAVENKRCK RYITVCGGTG CKSAEGDVIV
SNLKAEVEKA GLSEEVTVEI AGCFGFCEKG PIVKISPDNV FYVHVTPEDT QDIVNEHLLK
GKILENLLYE EPSVKEKVKR QDEMSFYKKQ HRIALRNCGF INPEDITESI ATKGYLALGK
CITEMSADDV VKLIIDSGLR GRGGGGFPTG KKWSFAKAYD ADQKYIICNA DEGDPGAFMD
RSILEGDPHS VLEAMAIAGY AIGASKGVIY IRAEYPLAVS RLKTAIDQAL ECGVLGNNIL
GSEFSFNIDI RYGAGAFVCG EETALIHSVE GCRGEPTNKP PFPAESGLWD KPTCVNNVET
LANIPAIINN GAEWYSSIGT ATSKGTKVFA LAGKINNVGL VEVPMGTTLR EIIYDIGGGI
KNGRKFKSVQ TGGPSGGCIP ASNLDIPIDY ESLTSIGSMM GSGGMIVMDE DNCMVDIAKF
YLEFTVEESC GKCTPCRIGN KRLLEILTKI TNGQGTEDDL EKLKELAQTI KDTSLCGLGQ
TAPNPILSTM KYFADEYEAH VKEKSCPAGV CKNLLKYEIT DKCIGCTKCL RNCPVNCING
KVKQVHTIDQ SKCIKCGACC SGCPVDAIVK K
//
