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Database: UniProt
Entry: D3RUD1_ALLVD
LinkDB: D3RUD1_ALLVD
Original site: D3RUD1_ALLVD 
ID   D3RUD1_ALLVD            Unreviewed;       538 AA.
AC   D3RUD1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=NADH dehydrogenase (Quinone) {ECO:0000313|EMBL:ADC62790.1};
DE            EC=1.6.5.11 {ECO:0000313|EMBL:ADC62790.1};
GN   OrderedLocusNames=Alvin_1865 {ECO:0000313|EMBL:ADC62790.1};
OS   Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS   10441 / D) (Chromatium vinosum).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=572477 {ECO:0000313|EMBL:ADC62790.1, ECO:0000313|Proteomes:UP000001441};
RN   [1] {ECO:0000313|EMBL:ADC62790.1, ECO:0000313|Proteomes:UP000001441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D
RC   {ECO:0000313|Proteomes:UP000001441};
RX   PubMed=22675582; DOI=10.4056/sigs.2335270;
RA   Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA   Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT   "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL   Stand. Genomic Sci. 5:311-330(2011).
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00007523}.
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DR   EMBL; CP001896; ADC62790.1; -; Genomic_DNA.
DR   RefSeq; WP_012971063.1; NC_013851.1.
DR   AlphaFoldDB; D3RUD1; -.
DR   STRING; 572477.Alvin_1865; -.
DR   KEGG; alv:Alvin_1865; -.
DR   eggNOG; COG1894; Bacteria.
DR   HOGENOM; CLU_014881_3_2_6; -.
DR   OrthoDB; 9805533at2; -.
DR   Proteomes; UP000001441; Chromosome.
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; 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; 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; 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; 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   Oxidoreductase {ECO:0000313|EMBL:ADC62790.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001441};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          448..493
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
SQ   SEQUENCE   538 AA;  57105 MW;  704CC7D2DB70178F CRC64;
     MHLEDLAEQA AQYRNEDAHI EREVRVCVAA SCQSSGSLPV LEALKSACDT QGAGSCKVKG
     VGCMGLCSAG PLVAVADKDC ALNESVLYRD VTPDDAPDIM ASVCSTPVER LRCPTDQPFF
     SRQQRIVLEH SGLIDPDSLR GYIAVGGYAA LVRALTEMTP ADVLREVTTS GLRGRGGGGY
     PTGLKWSTIA KMPPGQKYVV CNADEGDPGA FMDRAVLESD PHRVLEGMAI AAYAVGASKG
     YVYVRAEYPL AVERLETAIR KAKRAGFLGA KVADTQFAFE VEIRLGAGAF VCGEETALMA
     SIEGLRGQPR PRPPYPAESG LWGCPTLINN VETFANIAPI IREGGDWFAA IGTEGSKGTK
     VFALAGKIKN TGLIEVPMGT SLRDIIEVIG GGIPDGRAFK AVQTGGPSGG CIPEAHLDIP
     VDYDSLKTLG TIMGSGGLIV MDETSCMVDV ARFFMEFCMS ESCGKCIPCR AGTWQMHALL
     DTLTKGRGTR ADLALLEDLC DVVRATSLCG LGQTAPNPVL STLRYFRDEY EAKLLGDA
//
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