ID A0A106BJG8_THIDE Unreviewed; 608 AA.
AC A0A106BJG8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=NADP oxidoreductase {ECO:0000313|EMBL:KVW93492.1};
GN ORFNames=ABW22_13945 {ECO:0000313|EMBL:KVW93492.1};
OS Thiobacillus denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW93492.1, ECO:0000313|Proteomes:UP000064243};
RN [1] {ECO:0000313|EMBL:KVW93492.1, ECO:0000313|Proteomes:UP000064243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RG {ECO:0000313|EMBL:KVW93492.1,
RC ECO:0000313|Proteomes:UP000064243};
RX PubMed=26712544;
RA Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT Chemoautotroph.";
RL Appl. Environ. Microbiol. 82:1486-1495(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:KVW93492.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDUG01000046; KVW93492.1; -; Genomic_DNA.
DR RefSeq; WP_059757997.1; NZ_LDUG01000046.1.
DR AlphaFoldDB; A0A106BJG8; -.
DR PATRIC; fig|36861.3.peg.2610; -.
DR OrthoDB; 9805533at2; -.
DR Proteomes; UP000064243; 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 Gene3D; 3.10.20.600; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.10.10.1590; NADH-quinone oxidoreductase subunit E; 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; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR041921; NuoE_N.
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; PF10589; NADH_4Fe-4S; 1.
DR SMART; SM00928; NADH_4Fe-4S; 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; PS00644; COMPLEX1_51K_1; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000064243}.
FT DOMAIN 483..532
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 608 AA; 66063 MW; 254130AADCF0C831 CRC64;
MSIESAAFER VLSRHGRDPH ALVQILRETQ ALMGWLPRSL LSAMARELKL TLAHVEGVAG
FYRFFHTRPM GRLRVLFSDN ITDRMLGSEA LMADLCARLG IKPGQVSADG RVSVDQTSCT
GLCDQGPALL VNHHHVITRL DAPRVAQLAE LIRAEVPVPQ WPADWFAIDH NIRRADVLLG
MPLAPGAAIA AALARGAQAM LDDMKRSNLR GRGGAGFAAG LKWELCRNAT GSIPGTAPGS
THYVVCNADE GEPGTFKDRV LLARHADEVF EGMTVAALVI GARQGLLYLR GEYRYLLEHL
QAVLQRRRDQ NLLGSAILGR AGFDFDIAIH VGAGAYVCGE ESALIESLEG KRGTPRIRPP
FPVEQGYLGQ PTIVNNVETF CAASHIAAQG GAWWAGIGTH QSTGTKIHSV SGDCERPGLY
EYPFGTRIDQ ILEDCGARDT QAVQVGGPSG VCLSAFEFDR RIAFEDVPSA GAFMVFDCTR
DMFEVARNFA HFFAHESCGF CTPCRVGTAL VVKRLDKLAN ATGGGRGSRH DLDVLFELDL
LLHGTTHCGL GASACNPLRD TIIKFRPAYE RRLESLHFEP GFDLDAELSI ARRMTGRDDP
AAHLEISP
//
