ID   NUOD1_HERA2             Reviewed;         422 AA.
AC   A9B4Z7;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=NADH-quinone oxidoreductase subunit D 1 {ECO:0000255|HAMAP-Rule:MF_01358};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NADH dehydrogenase I subunit D 1 {ECO:0000255|HAMAP-Rule:MF_01358};
DE   AltName: Full=NDH-1 subunit D 1 {ECO:0000255|HAMAP-Rule:MF_01358};
GN   Name=nuoD1 {ECO:0000255|HAMAP-Rule:MF_01358}; OrderedLocusNames=Haur_3082;
OS   Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC   Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC   Herpetosiphon.
OX   NCBI_TaxID=316274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23779 / DSM 785 / 114-95;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_01358}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01358};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C,
CC       D, E, F, and G constitute the peripheral sector of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_01358}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01358};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01358};
CC       Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01358}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_01358}.
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DR   EMBL; CP000875; ABX05720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9B4Z7; -.
DR   SMR; A9B4Z7; -.
DR   STRING; 316274.Haur_3082; -.
DR   EnsemblBacteria; ABX05720; ABX05720; Haur_3082.
DR   KEGG; hau:Haur_3082; -.
DR   eggNOG; COG0649; Bacteria.
DR   HOGENOM; CLU_015134_1_2_0; -.
DR   OMA; IMGTSME; -.
DR   Proteomes; UP000000787; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.645.10; -; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993; PTHR11993; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; SSF56762; 1.
DR   TIGRFAMs; TIGR01962; NuoD; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW   Transport; Ubiquinone.
FT   CHAIN           1..422
FT                   /note="NADH-quinone oxidoreductase subunit D 1"
FT                   /id="PRO_0000357830"
SQ   SEQUENCE   422 AA;  47415 MW;  865581CF88DD23BD CRC64;
     MVMHAHAYPD IEIPTPSQIA AVALNNEPDE NGEQSMVLSM GPQHPSTHGV LRLAVELNGE
     NVVQLAPDVG FLHTGIEKTI ETKTYTKSIV LTDRMDYLAP MSNNMVYVAA IEKLMQQDVP
     ERAQTLRVLL LELTRINSHL VWLGTHALDL AAMSVFFYAM REREYILDIF EMLTGARMMT
     SYFRVGGLAW DIPADFIPTV EDFLTHFLPK VDEYEDLLTN NLLWKQRTKG VGVVNAADAI
     ALGLSGANLR ASGVDWDLRK TMPYSGYETY QFDVPVGQAG DIYDRYRCRV QEMRESVKIA
     RQAIERVKQM HGQPYVTENR KVAPPPKSEI TYSMESLIHH FKLWTEGFRP PRGSAYAAIE
     SPRGEIGCYV VSDGTPKPWR VHFRAPSFIN LQALPHIAKG KLMADLVALI ASIDPVLGEV
     DR