ID A0A1I7FEQ7_9BACT Unreviewed; 582 AA.
AC A0A1I7FEQ7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=NADH-quinone oxidoreductase subunit C/D {ECO:0000313|EMBL:SFU34586.1};
GN ORFNames=SAMN04487941_0143 {ECO:0000313|EMBL:SFU34586.1};
OS Pontibacter akesuensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=388950 {ECO:0000313|EMBL:SFU34586.1, ECO:0000313|Proteomes:UP000182491};
RN [1] {ECO:0000313|Proteomes:UP000182491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18820 {ECO:0000313|Proteomes:UP000182491};
RA Varghese 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
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; FPCA01000001; SFU34586.1; -; Genomic_DNA.
DR RefSeq; WP_068839146.1; NZ_FPCA01000001.1.
DR AlphaFoldDB; A0A1I7FEQ7; -.
DR STRING; 388950.GCA_001611675_03281; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000182491; Unassembled WGS sequence.
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:UP000182491};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 33..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; 66974 MW; 3E7155859E48FCB2 CRC64;
MENVSGTLEQ LQSRFGADTF TPQTTKDEIL TLWMPHGKIV EVLTYLKKEI SQPYLLLYDL
TATDERTRKP DNGHIPYAFT IIYHLFSFHR NSFIRLKVGY RDEFPVVPSI NTLWANANWY
EREVYDMFGI RFEGHPHLYR ILMPRTWVGH PLRKEHPARA TEMGPFALYD DKIDLEQSAL
QFKPEEWGLK RESDNSDFMF LNIGPQHPGT HGVLRIVLQL DGEDIVDAIP DIGFHHRGQE
KMAERQSWHT YLPYTDRVDY LGGVMNNLAY LLAVEKLAGI QVPERVKVIR VMLCELFRIA
SHLVWYGTFA QDVGQLSPVF YMFTDREKIF DIVEAVTGGR MHPNWFRIGG VAQDLPKGWE
LLVQNFLDYF PKRLKEYDNM VMKNSLFKAR TKGIGIFTTA EAIEWGVTGP NLRACGFDWD
FRKKQPYSGY ELFDFEVPTA ANGDCYDRAV VRVAEMRQSL RIIDQCLKNM PGGPYKADHP
LTTPPIKKHT MHDIETLITH FLGVSWGPVM PPGEAMSCIE ATKGANGYYV MSDGNTSPYR
LRIRTPSFPH MQMLPYITKG YTVADLLSIL GAMDYVLADI DR
//
