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Database: UniProt
Entry: A0A117R8T7_9ACTN
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ID   A0A117R8T7_9ACTN        Unreviewed;       383 AA.
AC   A0A117R8T7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=AQJ66_33720 {ECO:0000313|EMBL:KUN77385.1};
OS   Streptomyces bungoensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN77385.1, ECO:0000313|Proteomes:UP000053024};
RN   [1] {ECO:0000313|EMBL:KUN77385.1, ECO:0000313|Proteomes:UP000053024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN77385.1,
RC   ECO:0000313|Proteomes:UP000053024};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces bungoensis DSM 41781, type strain
RT   for the species Streptomyces bungoensis.";
RL   Submitted (OCT-2015) 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:KUN77385.1}.
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DR   EMBL; LMWX01000064; KUN77385.1; -; Genomic_DNA.
DR   RefSeq; WP_061929745.1; NZ_KQ948876.1.
DR   AlphaFoldDB; A0A117R8T7; -.
DR   STRING; 285568.AQJ66_33720; -.
DR   OrthoDB; 9801496at2; -.
DR   Proteomes; UP000053024; 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   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; 2.
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:UP000053024};
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          134..307
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
FT   DOMAIN          309..383
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
SQ   SEQUENCE   383 AA;  42271 MW;  E496C829FE26774F CRC64;
     MTPTTQTTVG IGGAAESTDM VLNIGPQHPS THGVLRLRLV LDGERIVRAD PVVGYMHRGA
     EKLFEARDYR QIIMLANRHD WLSAFSNELG VVLAVERMLG MEVPERAVWT RTLLAELNRV
     LNHLMFLGSY PLELGGITPV FYAFREREVL QNVMEEVSGG RMHYMFNRVG GLKEDLPAGW
     TARARAAVSA VRSRMDVFDD LVLGNEIFRG RTRGVGALAP EAVHAYGVSG PIARASGVDL
     DLRRDEPYLA YGELQDTLKV VTRGEGDCLA RFECLLEQTH NALDLADACL GRLAELPPGP
     INQRLPKVLK APEGHTYAWT ENPLGINGYY LVSKGEKTPY RLKLRSASYN NIQALTELLP
     GTLVADMVAI LGSMFFVVGD IDK
//
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