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Database: UniProt
Entry: F2JKP9_CELLD
LinkDB: F2JKP9_CELLD
Original site: F2JKP9_CELLD 
ID   F2JKP9_CELLD            Unreviewed;       624 AA.
AC   F2JKP9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:ADZ83302.1};
DE            EC=1.6.99.5 {ECO:0000313|EMBL:ADZ83302.1};
GN   OrderedLocusNames=Clole_1577 {ECO:0000313|EMBL:ADZ83302.1};
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:ADZ83302.1, ECO:0000313|Proteomes:UP000008467};
RN   [1] {ECO:0000313|EMBL:ADZ83302.1, 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}.
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DR   EMBL; CP002582; ADZ83302.1; -; Genomic_DNA.
DR   RefSeq; WP_013656600.1; NC_015275.1.
DR   AlphaFoldDB; F2JKP9; -.
DR   STRING; 642492.Clole_1577; -.
DR   KEGG; cle:Clole_1577; -.
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; PF12838; Fer4_7; 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:ADZ83302.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008467};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          567..596
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          597..624
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   624 AA;  68356 MW;  BF571F547CF21118 CRC64;
     MLKDRADLVQ MRIACKEALE LEKIKILVCS GTGCIASGSL EIYEEMLRLM KKEGLNCSVN
     LEEEPHDSSI GMKKSGCHGF CEMGPLLRIE PWGYLYIKVK VEDCKEIIEE TIKKGQCIER
     LIYKKDGKGY KTQAEIPFYK KQTRLVLEHC GHIDATSIKE YLAVGGYEAL EKALFDRDDE
     GIIHEITESN LRGRGGGGFP AGRKWTQVRR QVEPTKYVVC NGDEGDPGAF MDRSIMEGDP
     HRMLEGMMIA AKACKAREGY IYVRAEYPLA ISRLRKAIDE AREYGLLGEH ILGTDFSFDI
     KINRGAGAFV CGEGSALTAS IEGKRGMPRV KPPRTVEQGL FEKPTVLNNV ETFANVPLII
     LNGVDWYKGI GPEKSPGTKA FALTGNIENT GLIEVPMGTT LREVIFDIGG GMRDGANFKA
     VQIGGPSGGC LTSDDLDLPL DFDSLKKAGA MIGSGGLVVM DENTCMVEVA RFFMNFTQNE
     SCGKCVPCRE GTKRMLEILE RIVVGGGEEN DLDQLLELAD TISSTALCGL GKTAAFPVVS
     TIKKFKGEYL AHIVDKKCPS KTCQKLRQIY IDEVLCKGCS KCARSCPVGA ISGQIKKPFK
     IDEKKCIKCG ACIGACAFKA VKED
//
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