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Database: UniProt
Entry: H8KWJ7_SOLCM
LinkDB: H8KWJ7_SOLCM
Original site: H8KWJ7_SOLCM 
ID   H8KWJ7_SOLCM            Unreviewed;       582 AA.
AC   H8KWJ7;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=NADH dehydrogenase I, D subunit {ECO:0000313|EMBL:AFD08115.1};
GN   OrderedLocusNames=Solca_3102 {ECO:0000313|EMBL:AFD08115.1};
OS   Solitalea canadensis (strain ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB
OS   12057 / USAM 9D) (Flexibacter canadensis).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Solitalea.
OX   NCBI_TaxID=929556 {ECO:0000313|EMBL:AFD08115.1, ECO:0000313|Proteomes:UP000007590};
RN   [1] {ECO:0000313|Proteomes:UP000007590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB 12057 / USAM 9D
RC   {ECO:0000313|Proteomes:UP000007590};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Lu M.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Schroeder M., Kopitz M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Solitalea canadensis DSM 3403.";
RL   Submitted (FEB-2012) 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
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|ARBA:ARBA00002378}.
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|ARBA:ARBA00000100};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa
CC       subunit family. {ECO:0000256|ARBA:ARBA00010019}.
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DR   EMBL; CP003349; AFD08115.1; -; Genomic_DNA.
DR   RefSeq; WP_014681341.1; NC_017770.1.
DR   AlphaFoldDB; H8KWJ7; -.
DR   STRING; 929556.Solca_3102; -.
DR   KEGG; scn:Solca_3102; -.
DR   eggNOG; COG0649; Bacteria.
DR   eggNOG; COG0852; Bacteria.
DR   HOGENOM; CLU_015134_3_2_10; -.
DR   OrthoDB; 9801496at2; -.
DR   Proteomes; UP000007590; Chromosome.
DR   GO; GO:0030964; C:NADH dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR   Gene3D; 3.30.460.80; NADH:ubiquinone oxidoreductase, 30kDa subunit; 1.
DR   HAMAP; MF_01357; NDH1_NuoC; 1.
DR   HAMAP; MF_01359; NDH1_NuoCD_1; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR010218; NADH_DH_suC.
DR   InterPro; IPR023062; NADH_DH_suCD.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR   InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
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:SF45; NADH-QUINONE OXIDOREDUCTASE SUBUNIT C_D; 1.
DR   PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR   Pfam; PF00329; Complex1_30kDa; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   SUPFAM; SSF143243; Nqo5-like; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007590};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          32..161
FT                   /note="NADH:ubiquinone oxidoreductase 30kDa subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00329"
FT   DOMAIN          312..582
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
SQ   SEQUENCE   582 AA;  66992 MW;  9AB331B99F65C632 CRC64;
     MYAPEKLAPE LTLKFGESVL TPQQTADDVA TFWVHSTKVI EVLTYLKTGS PEPFPMLYDL
     FAIDERSRAN RNNYPSKDFT IVYHLLSFIR NQFIRLKIAL DGEYPSAPTL THLWPSAAWY
     EREVYDMFGI RFDGHPHLQR ILMPLTWQGH PLRKEHPARA TEMGPFKLWD EKVDTEQGAL
     RFKPEEWGLK RHSEDADFMF LNIGPQHPGT HGVLRIILQL DGEDIIDAVP DIGFHHRGAE
     KMGERQSWHT YIPYTDRIDY LGGVMNNLAY LLSVEKLAGI EVPERVKVIR VMMCEFFRIA
     SHLVWYGTFA QDIGQLSPVF YMFTDREKIF DIVEAVCGGR MHPNWFRIGG VSQDLPKGWD
     KLVADFIAYF PKRVKEYHNM VMKNSIFKAR TVGIGIYTLQ EAIEWGVTGP GLRACGFEWD
     MRKKQPYSGY ENFDFEIPIA QNGDCYDRAV VRELEMLQSL RIIEQCLKHM PEGAFKADHP
     LTTPPLKKYT MQDIETLINH FLNVSWGPVI PTGEAMSCIE ATKGNNSYYM VSDGNTSPYR
     SRIRTPSFPH MQMLPYISKG YTVADLLSIL GSMDYVLADI DR
//
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