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Database: UniProt
Entry: A0A286IPU7_9BACT
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ID   A0A286IPU7_9BACT        Unreviewed;       413 AA.
AC   A0A286IPU7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=NADH-quinone oxidoreductase subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01358};
DE   AltName: Full=NADH dehydrogenase I subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
DE   AltName: Full=NDH-1 subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
GN   Name=nuoD {ECO:0000256|HAMAP-Rule:MF_01358};
GN   ORFNames=SAMN06298216_3069 {ECO:0000313|EMBL:SOE22654.1};
OS   Spirosomataceae bacterium TFI 002.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae.
OX   NCBI_TaxID=1945892 {ECO:0000313|EMBL:SOE22654.1, ECO:0000313|Proteomes:UP000217493};
RN   [1] {ECO:0000313|EMBL:SOE22654.1, ECO:0000313|Proteomes:UP000217493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TFI 002 {ECO:0000313|EMBL:SOE22654.1,
RC   ECO:0000313|Proteomes:UP000217493};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) 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 a
CC       menaquinone. 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01358}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01358};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01358};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01358}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|HAMAP-Rule:MF_01358,
CC       ECO:0000256|RuleBase:RU003685}.
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DR   EMBL; LT907983; SOE22654.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286IPU7; -.
DR   OrthoDB; 9801496at2; -.
DR   Proteomes; UP000217493; Chromosome i.
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; Cytochrome-c3 Hydrogenase, chain B; 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   NCBIfam; TIGR01962; NuoD; 1.
DR   PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01358};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217493};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_01358};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01358}.
FT   DOMAIN          142..412
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
SQ   SEQUENCE   413 AA;  47135 MW;  834943BBF8C1EA15 CRC64;
     MADQEIHIAR NTSDALALNL PIEEERELTT LNLGPTHPAT HGIFQNVLQM DGDKIVSGEQ
     TVGYIHRAFE KIAERRPFYQ ITTLTDRMNY CSSPINNFGW HMTVEKLLEV EVPKRAQYIR
     VIMMELARIS DHLICNSILG VDTGAYSGFL HIFQEREKIY EVYEEVCGAR LTTNMGRIGG
     MERDLSPTAL KKIKDIVYNS FPKALAEFER LMNRNRIFMD RTINVGKITG ERAMEYGFTG
     PNLRAAGVDY DVRAMEPYSS YEDFDFEIPI GHNGDTYDRY MVRNAEMWES IKIIKQALEN
     LPGGPFYANE DHYYLPPKKD VYRSMEALIY HFKIIMGEID APIGEVYHAV EGGNGELGFY
     LISDGGRTPF RLHFRRPSFI YYQAYSEMCK GLTISDAVAI MSSLNVIAGE LDA
//
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