ID F2JSY1_CELLD Unreviewed; 595 AA.
AC F2JSY1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:ADZ84102.1};
DE EC=1.6.99.5 {ECO:0000313|EMBL:ADZ84102.1};
GN OrderedLocusNames=Clole_2395 {ECO:0000313|EMBL:ADZ84102.1};
OS Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS RHM5) (Clostridium lentocellum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC Cellulosilyticum.
OX NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ84102.1, ECO:0000313|Proteomes:UP000008467};
RN [1] {ECO:0000313|EMBL:ADZ84102.1, ECO:0000313|Proteomes:UP000008467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC {ECO:0000313|Proteomes:UP000008467};
RX PubMed=21398547; DOI=10.1128/JB.00239-11;
RG US DOE Joint Genome Institute;
RA Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA Angert E.R., Currie C.R.;
RT "Complete genome sequence of the cellulose-degrading bacterium
RT Cellulosilyticum lentocellum.";
RL J. Bacteriol. 193:2357-2358(2011).
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002582; ADZ84102.1; -; Genomic_DNA.
DR RefSeq; WP_013657395.1; NC_015275.1.
DR AlphaFoldDB; F2JSY1; -.
DR STRING; 642492.Clole_2395; -.
DR KEGG; cle:Clole_2395; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_3_2_9; -.
DR Proteomes; UP000008467; 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; -; 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; 2.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:ADZ84102.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008467};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 537..567
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 568..595
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 595 AA; 64579 MW; F9835A06531E3BDC CRC64;
MSKYTMHILV CGGTGCLSSQ SNEIVDQLIA HIEEAGMSEE VQVLKTGCFG FCEKGPIVKI
LPDNTFYVQV KPEDAEEIVK EHIVKGRKVP RLLYEDPTTE EHVSDSKHMD FYKKQMRVAL
RNCGFIDPDN IEEYIARDGY AALAKVLTMT QEEVINEVKA SGLRGRGGGG FPTGLKWEFA
YKNKADQKYV VCNADEGDPG AFMDRSILEG DPNSIVEAMA ICGYAIGATK GLVYIRAEYP
LAIKRLESAI HSAREYGLLG DNIMGSDFCF DIDIRFGAGA FVCGEETALI HSMEGMRGEP
TTKPPFPAAS GYWGKPTNVN NVETFANIPV IILKGAEWFS KIGTEKSKGT KVFALAGKIN
NVGLIEVPMG ITLREVIYDI GGGIKNGKQF KAVQTGGPSG GCLTVKDLDT PIDFDNLIAK
GSMMGSGGMI VLDEDDCMPA VAKFYLEFTA EESCGKCTPC RIGTKRLLEI LEKITAGKGS
EEDLKVLKEL SEVIKDTALC GLGQTAPNPV LSTLTTFEDE YLAHIYDHKC PAGQCTALLQ
YHITEQCKGC TACARVCPVG AISGTVKALH TIDQEKCIKC GACMDKCKFA AIVRE
//
