ID B8FFJ2_DESAL Unreviewed; 1044 AA.
AC B8FFJ2;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=NADH:ubiquinone oxidoreductase, NADH-binding subunit (NuoF-like) {ECO:0000313|EMBL:ACL04252.1};
GN OrderedLocusNames=Dalk_2559 {ECO:0000313|EMBL:ACL04252.1};
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfatibacillaceae; Desulfatibacillum.
OX NCBI_TaxID=218208 {ECO:0000313|EMBL:ACL04252.1, ECO:0000313|Proteomes:UP000000739};
RN [1] {ECO:0000313|EMBL:ACL04252.1, ECO:0000313|Proteomes:UP000000739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01 {ECO:0000313|EMBL:ACL04252.1,
RC ECO:0000313|Proteomes:UP000000739};
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
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DR EMBL; CP001322; ACL04252.1; -; Genomic_DNA.
DR RefSeq; WP_015947325.1; NC_011768.1.
DR AlphaFoldDB; B8FFJ2; -.
DR KEGG; dal:Dalk_2559; -.
DR eggNOG; COG0493; Bacteria.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_010449_1_0_7; -.
DR Proteomes; UP000000739; 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; 6.10.250.1450; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
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; PF14691; Fer4_20; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF10531; SLBB; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 2.
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; SSF51971; Nucleotide-binding domain; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000000739};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 459..504
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 1044 AA; 113505 MW; 7FF498598BDEB77F CRC64;
MNKLTSIGQM EWLRNKTQAA LSQARNVIHV CMTGCRAYGA AEVLQSLQDE VKRQGMEKEV
EVRSTGCHGF CARAPVIALD PLGVQYQEVG PEDAAEIIGQ TIKQNRLIDR LAYKEPKTNK
PIYYRDQIPF YMKQERRVLA LCGRIDPTSI EHYIAAGGYQ ALVRVLSGMA PEQVAQEVID
AKLRGRGGAG FPAGLKWKFA RQSSANPKYI ICNADEGDPG AFMDRAILEG DPHSVIEGMI
IGAFAMGARY GFIYVREEYP IAVEHLNCAI AQAGELGILG ENILGTGFSF SLSLKMGAGA
FVCGEETALM ASIEGKRGMP RARPPFPAQS GVDGKPSNIN NVETFANVPL ILKNGAGWYA
QVGTENSKGT KIFSLAGKVN NTGLVEVPIG TSIREVVFDI GGGIPKGRKF KAVQMGGPSG
GCVPAQFLNL SIDYDTLQKI GAIMGSGGMV VMDENNCMVE IARFFLAFTQ SESCGKCSPC
RLGTTQLLEI LTRITTGRGR LEDIETIKEI GRTMTEASLC GLGQNCAKPA ISTLQYFLKE
YEDHILENRC AGAVCKSMVI SACQHACPAG IDVPNYVAAI ARGRFQDAVD IIRERNPFPA
VCGRICIHPC EFKCRRGELD EPVAIRLLKR FATDWYFDNM GVEAEPFPVT REEKVAVVGA
GPAGLTCAYF LAEMGYKATV FEAAPKGGGM LGITVPEFRL PRHVIEQEIQ YIRNKGVEIQ
YNSPIDANHT VNDLMASGYK AVFIAAGAQA SKTIGIPGEE EDLNGLFYGL QFLTQVKGED
AVSLSGRAVV IGGGNVAIDV ARTALRVGAS DVQVFCLESF DQMPAWDKEV DEAMEEGIVI
NPSWSPRLIV SEAGKVQGVE FSRCDSVFDD DGKFNPTCDD STIRMVEAEN VIISIGQAAD
MSFLSQDEQL ERALWGTLAV DENRLATNIP GIFAGGDFTT GPTFVIRAIS SGRRAAIAID
KYLSGDEGRV HTPDRKTRLI QDAGLALEDE EGGKEAPRVK VALEDRQERA HDFREIEKGF
TREQALREAV RCLRCDLERE EEAS
//
