ID A0A238KZN8_9RHOB Unreviewed; 567 AA.
AC A0A238KZN8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 18-JUN-2025, entry version 28.
DE SubName: Full=NADH-quinone oxidoreductase subunit 1 {ECO:0000313|EMBL:SMX47556.1};
DE EC=1.6.5.11 {ECO:0000313|EMBL:SMX47556.1};
GN Name=nqo1_1 {ECO:0000313|EMBL:SMX47556.1};
GN ORFNames=RUA8715_03117 {ECO:0000313|EMBL:SMX47556.1};
OS Ruegeria arenilitoris.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1173585 {ECO:0000313|EMBL:SMX47556.1, ECO:0000313|Proteomes:UP000202485};
RN [1] {ECO:0000313|Proteomes:UP000202485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8715 {ECO:0000313|Proteomes:UP000202485};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523}.
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DR EMBL; FXYG01000004; SMX47556.1; -; Genomic_DNA.
DR RefSeq; WP_093965020.1; NZ_FXYG01000004.1.
DR AlphaFoldDB; A0A238KZN8; -.
DR OrthoDB; 9761899at2; -.
DR Proteomes; UP000202485; 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; cd03082; TRX_Fd_NuoE_W_FDH_beta; 1.
DR FunFam; 3.10.20.600:FF:000006; Formate dehydrogenase, beta subunit; 1.
DR FunFam; 3.40.50.11540:FF:000003; NAD-dependent formate dehydrogenase flavoprotein subunit; 1.
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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:SMX47556.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000202485}.
FT DOMAIN 491..536
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..28
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 61663 MW; FD6B3D98E34A8E06 CRC64;
MAPLDTKPSG APKGVWKSGK GKGRHTPKGR QFTDEAQAEI QRLLGDRPRR RDLLIEFLHL
IQDTHGHISA DHIAALAVEM RIGQAEIYET ATFYAHFDVV KEGETPPPAL TIRVCDSLSC
EMAGAQQLKK ALEDGLDPSE VRVLRAPCMG RCDTAPVLEI GHNQIDHATP EKVQAAVAAG
DTHAHLPDYE TFATYVESGG YAKLKELREG GDWEAVQEQV LASGLRGLGG AGFPSGKKWG
FVRMNDGPRY LAVNGDEGEP GTFKDRYYLE RTPHVFLEGM LIAAWAVEAE TCFIYMRDEY
PAVLEILRRE IAALEQDGIV EKGYIDLRRG AGAYICGEES AMIESIEGRK GLPRHRPPFV
AQVGVFGRPT LVHNVETLHW VSKICREGPE ILSSVEKNGR KGLRSYSVSG RVAKPGVYLL
PAGSTILDVI DAAGGMAEGH VFKAYQPGGP SSGLLPSSID DVPLDFDTLQ PLGTFIGSAA
VVVLSDQDTA RDAALNMLRF FEDESCGQCT PCRAGCEKAV KLMQADKWDT DLLEDLCQVM
GDASICGLGQ AAPNPIRLVM KHFADEI
//
