ID A0A1F8MBF3_9CHLR Unreviewed; 617 AA.
AC A0A1F8MBF3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:OGN95967.1};
GN ORFNames=A2Y89_00780 {ECO:0000313|EMBL:OGN95967.1};
OS Chloroflexi bacterium RBG_13_51_18.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797624 {ECO:0000313|EMBL:OGN95967.1, ECO:0000313|Proteomes:UP000180314};
RN [1] {ECO:0000313|EMBL:OGN95967.1, ECO:0000313|Proteomes:UP000180314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGN95967.1}.
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DR EMBL; MGMR01000086; OGN95967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8MBF3; -.
DR Proteomes; UP000180314; 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; 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; 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 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; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 560..589
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 590..617
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 617 AA; 66725 MW; 7BB621AE081973A3 CRC64;
MLRLNSYREL EHLREQLRQQ RQVYKTTVMI CGGTGCQASR SSSVIEAIRS ELSKQGLTDS
VRLCVTGCHG FCEQGPVMII EPGNIFYCQV TPEDVFEIVF HTFVKGKVVE RLLYKDMVSG
KSYQMETEIP FYRAQDRQIL SQNLNVDPCS VEDYIISGGY SALTKVLSGV SPEEIIKEIK
SSGLRGRGGG GFPTGNKWSE CREAPSAEKY VICNADEGDP GAYMDRCVLE GNPHLILEGM
MIGAWAVGAS KGYIYVRNEY PLAVKHSRIA VKQARELGLL GENILGSALS FDVEIARGGG
AFVCGESTAL MASVEGKVGE PRPKDVHTVV DGLYHKPTTL NNVETWANVP AIMLKGSSWF
ASKGTQGSKG TKILALTGRI KNTGLVEVAM GTPIRTVVFD IGGGAVDGKA IKAVQTGGPS
GGCLPVDKFD LAIDFDILAE AGSMVGSGGM VVMDEGSCMV DVAKYFLTFL QDESCGKCVP
CRLGIDRMLE IITDITEGRG RPEQIDLLEE LADTISQTAL CGLGKTAPNP VISTLRYFRS
EYEAHINNKK CPAGVCKSLI TYSIDPEKCT GCGICLRVCS RKAITGEKKE PHVIDTELCQ
KCGVCISECK FDAIKVA
//
