ID A0A238DHL2_9BURK Unreviewed; 634 AA.
AC A0A238DHL2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:SCC91011.1};
GN ORFNames=THIX_10052 {ECO:0000313|EMBL:SCC91011.1};
OS Thiomonas sp. X19.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=1050370 {ECO:0000313|EMBL:SCC91011.1, ECO:0000313|Proteomes:UP000250096};
RN [1] {ECO:0000313|EMBL:SCC91011.1, ECO:0000313|Proteomes:UP000250096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X19 {ECO:0000313|EMBL:SCC91011.1,
RC ECO:0000313|Proteomes:UP000250096};
RA Regsiter A., william w.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:SCC91011.1}.
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DR EMBL; FMBP01000001; SCC91011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238DHL2; -.
DR OrthoDB; 9805533at2; -.
DR Proteomes; UP000250096; Chromosome thix.
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; 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; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF10531; SLBB; 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 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:UP000250096};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 549..594
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 634 AA; 67079 MW; E365C92043024F12 CRC64;
MSTTAPTRVP TAVEPQQSAA RPQPLRFMRN TPRGGLVSPQ ARQAVQAACA DLAARPDLLM
EHLHRINDAE GGLRPSRLAA LAEWLRLSTS EVFEVASFYH HFRLLREDEP APTATVRVCT
NLSCALAGAD ALLTDLQQRC GDGVAVEGAS CMGLCTRAPG VLVGRQALGH ATAEAVLAAL
PQAIPLPAFP AGGEGEITPS QPVGRIGVGN VAPPAPKDAE DLAAYRAGGG YALLADCRAG
RITPEVAMQR IEDAELRGLG GAGFPSVRKW RTVAQQPGPR LVVINADEGE VGTCKDGHLL
RTTPHRMLEG ILIAAWAVAA GRVWIYLRDE YAAEGALLHR ELQALHAAGL LRYGGVDIGG
AADDEPGSDA EVRKRLPQVA LRRGAGAYIC GEESALIESL EGKRGMPRLK PPIVAISGLF
GRPTLEHNVE TLWWVRDILN DPLAWANQGR RGRKGLRRFT VSGRVAKPGV VLAPAGITSR
ELIDEYCGGM ATGWTLYGVL PGGASGGILN ESQADLPLDF GTLDAQGCFI GSMAVIVLGR
NPHHTDTATH AARNLMQFFA HESCGQCTPC REGTHQMLAA MAPSQWDGAH IGALSQLMRD
ASICGLGQAA PNPTDSVLRH FPQEVGSGRA TAEI
//
