ID S4SZH9_MEDTR Unreviewed; 393 AA.
AC S4SZH9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=ndhH {ECO:0000313|EMBL:AFR59927.1};
GN Synonyms=nuoD {ECO:0000256|HAMAP-Rule:MF_01358};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OG Plastid {ECO:0000313|EMBL:AFR59927.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:AFR59927.1};
RN [1] {ECO:0000313|EMBL:AFR59927.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Paraggio {ECO:0000313|Proteomes:UP000002051};
RX PubMed=24644300; DOI=10.1093/dnares/dsu007;
RA Gurdon C., Maliga P.;
RT "Two Distinct Plastid Genome Configurations and Unprecedented Intraspecies
RT Length Variation in the accD Coding Region in Medicago truncatula.";
RL DNA Res. 21:417-427(2014).
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: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; JX512022; AFR59927.1; -; Genomic_DNA.
DR EMBL; JX512023; AFR60003.1; -; Genomic_DNA.
DR EMBL; JX512024; AFR60079.1; -; Genomic_DNA.
DR RefSeq; YP_001381680.1; NC_003119.6.
DR AlphaFoldDB; S4SZH9; -.
DR STRING; 3880.S4SZH9; -.
DR GeneID; 5333202; -.
DR KEGG; mtr:5333202; -.
DR OrthoDB; 191at2759; -.
DR Proteomes; UP000002051; Plastid.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
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 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 Plastid {ECO:0000313|EMBL:AFR59927.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
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};
KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01358}.
FT DOMAIN 124..393
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
SQ SEQUENCE 393 AA; 45725 MW; FA2A90F8A1044FA2 CRC64;
MNVPATRKDL MIVNMGPQHP SMHGVLRLIV TLDGEDVIDC EPILGYLHRG MEKIAENRTI
IQYLPYVTRW DYLATMFTEA ITVNGPEQLG NIQVPKRASY IRVIMLELSR IASHLLWLGP
FMADIGAQTP FFYIFREREL IYDLFEAATG MRMMHNYFRI GGVAADLPYG WIDKCFDFCN
YFLTRVIEYQ KLITRNPIFL ERVEAVGVVG REEVINWGLS GPMLRASGIQ WDLRKVDNYE
CYEEFDWEVQ WQKEGDSLAR YLVRIGEMME SIKIIQQALE GIPGGPYENL EIRSFDREKE
PEWNDFEYRF IGKKSSPTFE LPKQELYVRV EAPKGELGIF LLGDQNGFPW RWKIRPPGFI
NLQILPQLVK RMKLADIMTI LGSIDIIMGE VDR
//
