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Database: UniProt
Entry: A0A3R7FBT3_9ACTN
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ID   A0A3R7FBT3_9ACTN        Unreviewed;       440 AA.
AC   A0A3R7FBT3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=DC095_020785 {ECO:0000313|EMBL:RNC72078.1}, SFRA_018585
GN   {ECO:0000313|EMBL:RKM94479.1};
OS   Streptomyces xinghaiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1038928 {ECO:0000313|EMBL:RKM94479.1, ECO:0000313|Proteomes:UP000028058};
RN   [1] {ECO:0000313|EMBL:RKM94479.1, ECO:0000313|Proteomes:UP000028058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19609 {ECO:0000313|EMBL:RKM94479.1,
RC   ECO:0000313|Proteomes:UP000028058};
RX   PubMed=25477406;
RA   Bekker O.B., Klimina K.M., Vatlin A.A., Zakharevich N.V., Kasianov A.S.,
RA   Danilenko V.N.;
RT   "Draft Genome Sequence of Streptomyces fradiae ATCC 19609, a Strain Highly
RT   Sensitive to Antibiotics.";
RL   Genome Announc. 2:0-0(2014).
RN   [2] {ECO:0000313|EMBL:RKM94479.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 19609 {ECO:0000313|EMBL:RKM94479.1};
RA   Danilenko V.N., Bekker O.B., Vatlin A.;
RT   "Genome sequencing of Streptomyces fradiae ATCC 19609.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:RNC72078.1, ECO:0000313|Proteomes:UP000245280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OlgR {ECO:0000313|EMBL:RNC72078.1,
RC   ECO:0000313|Proteomes:UP000245280};
RA   Danilenko V.N., Bekker O.B., Vatlin A.;
RT   "Genome sequencing of Streptomyces xinghaiensis (fradiae) OlgR.";
RL   Submitted (OCT-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RKM94479.1}.
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DR   EMBL; JNAD02000008; RKM94479.1; -; Genomic_DNA.
DR   EMBL; QFBD02000009; RNC72078.1; -; Genomic_DNA.
DR   RefSeq; WP_043469352.1; NZ_QFBD02000009.1.
DR   AlphaFoldDB; A0A3R7FBT3; -.
DR   OrthoDB; 9801496at2; -.
DR   Proteomes; UP000028058; Unassembled WGS sequence.
DR   Proteomes; UP000245280; Unassembled WGS sequence.
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   Oxidoreductase {ECO:0000313|EMBL:RKM94479.1};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028058};
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          155..440
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
SQ   SEQUENCE   440 AA;  48269 MW;  6C129E641E4B5E85 CRC64;
     MTTSHAQERE TTEGKVYTVT GGDWDELAQA AAQADDERII VNMGPQHPST HGVLRLILEI
     DGETVTEARC GIGYLHTGIE KNLEYRTWTQ GTTFVTRMDY LTPFFNETAY CLGVEKLLGI
     EADIPDRASV IRVMMMELNR ISSHLVALAT GGMELGATTI MIYGFRDREL VLDLFELITG
     LRMNHAYIRP GGLAQDLPAG TVDAVREFIK QMRKNLPEYD ALATGNPIFK ARLQGIGHLD
     LTGCMSLGVT GPVLRSTGLP HDLRKADPYC GYETYDFEVA TADTSDSYGR FLIRLEEMRQ
     SLRIVEQCLD RLEPGPVMVA DKKIAWPAQL ALGPDGLGNS LDHIKKIMGT SMEALIHHFK
     LVTEGFRVPP GEAYTAVESP KGELGVHVVS DGGTRPYRVH FRDPSFTNLQ AVAAMCEGGQ
     VADVIVAVAS LDPVMGGVDR
//
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