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Database: UniProt
Entry: A0A0S7XNS2_9BACT
LinkDB: A0A0S7XNS2_9BACT
Original site: A0A0S7XNS2_9BACT 
ID   A0A0S7XNS2_9BACT        Unreviewed;      1048 AA.
AC   A0A0S7XNS2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=NADH-ubiquinone oxidoreductase 51kDa subunit iron-sulphur binding domain-containing protein {ECO:0000259|SMART:SM00928};
GN   ORFNames=AMK68_02235 {ECO:0000313|EMBL:KPJ64145.1};
OS   candidate division KD3-62 bacterium DG_56.
OC   Bacteria; candidate division KD3-62.
OX   NCBI_TaxID=1704032 {ECO:0000313|EMBL:KPJ64145.1, ECO:0000313|Proteomes:UP000052020};
RN   [1] {ECO:0000313|EMBL:KPJ64145.1, ECO:0000313|Proteomes:UP000052020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG_56 {ECO:0000313|EMBL:KPJ64145.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPJ64145.1}.
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DR   EMBL; LIZY01000040; KPJ64145.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S7XNS2; -.
DR   PATRIC; fig|1704032.3.peg.239; -.
DR   Proteomes; UP000052020; 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; 6.10.250.1450; -; 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   Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 1.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
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; 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; PR00419; ADXRDTASE.
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; 1.
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   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   1048 AA;  111344 MW;  D4ED4A8BE8D428FD CRC64;
     MSLADLQAPA QENWQKLKHG PDPIIWSGLA TCGLAAGQAE VLDAVAAALE HNAIRAQVVP
     VGCIGVCYLE PLMDIEKPGG PRICYAQMTP DKARAVIQSY LVNDDPRPDL ALGTLGDGEI
     AGIPRFFDLP MLKSQVRIVL RNVGLINPED IDHYIASGGY QGFQQALSMA PEAVIDEVTE
     SGLRGRGGAG FPTGQKWRFA RQASGSPKYL ICNADEGDPG AFMDRSVLEG DPHSVLEGML
     IAGYAIGASE GYIYVRSEYP LAIKRMSIAL EQMRNCGLLG ENILGSGFDF DIKIKEGAGA
     FVCGEETALI ASIEGKRGMP NPRPPFPATS GLWGKPTNIN NVETFANLPV ILSRGADWFA
     SYGTEKSKGT KTFSLTGKVK RSGLIEVPMG MSLGDVIFSI GGGIVDDGEL KAVQSGGPSG
     GCLPARLANL PIEYESLAEA GSIMGSGGLV VLDDKTCVVD MARYFLSFTQ RESCGKCVPC
     RLGTKQMEAI LEDICAGRGT PEHVTLLTDL ARAVKAGSLC GLGQTAPNPV LSTLRYFQDE
     YDAHIREKRC PAAACWGLFR SPCQHACPVG VDVPGYVGMI AEGRFAEAVD LVRERNPFPA
     ICGRVCTHPC ESRCQRAQID DPIAICSLKR AAADFAAASG HLWQPPLAPS NGRKVAIIGG
     GPAGLTAAYH LRKRGYAPTV FEAANRLGGM LRWGIPGYRL PDDVLDKEIA DIVGLGIDVR
     TGHAWGRDFT LPGLREQGYE AILLAIGAHH GVDLGMPGEA LEGVVDGVRF LRHVNSDEGM
     RLDGRRVVVI GGGDVAIDAA RSALRLGADK VSLVYRRTRA EMPAHASEIA AAEEEGVELQ
     FLLAPQRVVG SDRATGLECL RMSLGEFDDS GRRRPEPVPG SETVIEADLI ITAIGQTSDV
     PLDDRGGLAV SRRGAIEACA NSLVTGADGV FAAGDAVTGP DTVIRAIAQG ERAAIAIDRY
     LRGKTLAEEA ILVGHAPPQS SGEATDEEAE EEIKECPRAI MPCLDVERRT ALFAEVAQGF
     DREQAIAEAN RCLHCERSSH AEPEGGEG
//
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