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Database: UniProt
Entry: A0A1H3DND7_9FLAO
LinkDB: A0A1H3DND7_9FLAO
Original site: A0A1H3DND7_9FLAO 
ID   A0A1H3DND7_9FLAO        Unreviewed;       373 AA.
AC   A0A1H3DND7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=SAMN05444411_10822 {ECO:0000313|EMBL:SDX68032.1};
OS   Lutibacter oricola.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lutibacter.
OX   NCBI_TaxID=762486 {ECO:0000313|EMBL:SDX68032.1, ECO:0000313|Proteomes:UP000199595};
RN   [1] {ECO:0000313|EMBL:SDX68032.1, ECO:0000313|Proteomes:UP000199595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24956 {ECO:0000313|EMBL:SDX68032.1,
RC   ECO:0000313|Proteomes:UP000199595};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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|HAMAP-Rule:MF_01358}.
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DR   EMBL; FNNJ01000008; SDX68032.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3DND7; -.
DR   STRING; 762486.SAMN05444411_10822; -.
DR   Proteomes; UP000199595; 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; 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.
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|HAMAP-Rule:MF_01358};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199595};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01358}.
FT   DOMAIN          128..373
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
SQ   SEQUENCE   373 AA;  42079 MW;  618D30FE8A1CDF7E CRC64;
     MDTNIANSNL KSEDYFINMG PQHPATHGVL RLLLTIDGEI IKKVEPDLGY IHRSIEKMSE
     RDSYQQIVHL TDRMDYLSSH INNEAVCLTV ENALEIEVPE RVKVIRTIIG ELTRIASHCL
     WWGVMGMDVG ALTTYFYGFR DREMINDIFE ETCGARLTMN YNIPGGLMFD IHPNFVKRTK
     EFVAHFKTKI PEYDKLLTGN VIFQKRMKGV GILSKEDAIS FGASGPVARG SGYSCDVRKY
     YPYSALDKVT FNEALKTDGD SLARYEVRIQ EMWESLSIIE QLIDNIPEGD YKVATKAVIK
     LPKGEFYQKV ETARGELGVF INSTGTKNPY RLKFRSPGFS NLSLLNHIAV GGKIGDLVAS
     MATLDLVIPD IDR
//
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