ID A0A101GI50_9BACT Unreviewed; 597 AA.
AC A0A101GI50;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:KUK58605.1};
GN ORFNames=XD80_0726 {ECO:0000313|EMBL:KUK58605.1};
OS Synergistales bacterium 53_16.
OC Bacteria; Synergistota; Synergistia; Synergistales.
OX NCBI_TaxID=1635273 {ECO:0000313|EMBL:KUK58605.1, ECO:0000313|Proteomes:UP000053116};
RN [1] {ECO:0000313|Proteomes:UP000053116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(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:KUK58605.1}.
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DR EMBL; LGGB01000036; KUK58605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101GI50; -.
DR PATRIC; fig|1635273.3.peg.240; -.
DR Proteomes; UP000053116; 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; -; 2.
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.
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 540..569
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 570..597
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 597 AA; 65690 MW; 18DA55DB8EB5D39B CRC64;
MALYRAHVLI CKGTGCTASG ASSVYSAMQE ELRRRKLDSE IMLVETGCHG MCEMGPIVVV
YPEGAFYCRV TPEDVPEIVE EHLYKGRLVE RLLYTAPSDM TKIPHYRDIP FYSKQHRIVL
KNCGYINPEH IEEYISRDGY QALAKALLKM TPEKTLEEVK KSGLRGRGGA GFPTGLKWEF
ARKAPGDKKY VICNADEGDP GAFMDRSVLE GDPHSLIEGM LLGAYAIGAD EGYIYCRAEY
PLAIKRLKNA IAQAEEFGLL GDRIMGTDFS FHLHIKEGAG AFVCGEETAL MASIEGKRGM
PTPRPPFPAQ HGLWGKPTNI NNVETWANVP QIILNGAEWY SNIGTEKSKG TKVFALTGKV
KNTGLIEVPM GITIREIVFE LGGGILNDKG FKAVQIGGPS GGCLTKEHLD LPVDYESLTA
AGAIMGSGGL VVMDEDTCMV DVAKFFLEFT QRESCGKCVP CREGTKQMLL LLEKITKGEG
TMEDLETLEE LAHMVQRMSL CGLGQTAPNP VLTTLRYFRD EYEAHIKDRE CPAKACTALI
AYTIDPEKCK KCGLCAKNCP VNCIAGDRQT PYKIDQERCI KCGTCLEVCP FNAVHKD
//