ID B8KTH8_9GAMM Unreviewed; 592 AA.
AC B8KTH8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=NADH-quinone oxidoreductase subunit C/D {ECO:0000256|HAMAP-Rule:MF_01359};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01359};
DE AltName: Full=NADH dehydrogenase I subunit C/D {ECO:0000256|HAMAP-Rule:MF_01359};
DE AltName: Full=NDH-1 subunit C/D {ECO:0000256|HAMAP-Rule:MF_01359};
GN Name=nuoBCD {ECO:0000313|EMBL:EED34779.1};
GN Synonyms=nuoC {ECO:0000256|HAMAP-Rule:MF_01359}, nuoCD
GN {ECO:0000256|HAMAP-Rule:MF_01359}, nuoD
GN {ECO:0000256|HAMAP-Rule:MF_01359};
GN ORFNames=NOR51B_718 {ECO:0000313|EMBL:EED34779.1};
OS Luminiphilus syltensis NOR5-1B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Luminiphilus.
OX NCBI_TaxID=565045 {ECO:0000313|EMBL:EED34779.1, ECO:0000313|Proteomes:UP000004699};
RN [1] {ECO:0000313|Proteomes:UP000004699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NOR51-B {ECO:0000313|Proteomes:UP000004699};
RX PubMed=23705883;
RA Spring S., Riedel T., Sproer C., Yan S., Harder J., Fuchs B.M.;
RT "Taxonomy and evolution of bacteriochlorophyll a-containing members of the
RT OM60/NOR5 clade of marine gammaproteobacteria: description of Luminiphilus
RT syltensis gen. nov., sp. nov., reclassification of Haliea rubra as
RT Pseudohaliea rubra gen. nov., comb. nov., and emendation of Chromatocurvus
RT halotolerans.";
RL BMC Microbiol. 13:118-118(2013).
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 ECO:0000256|HAMAP-Rule:MF_01359}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01359};
CC -!- SUBUNIT: NDH-1 is composed of 13 different subunits. Subunits NuoB, CD,
CC E, F, and G constitute the peripheral sector of the complex.
CC {ECO:0000256|HAMAP-Rule:MF_01359}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01359};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01359};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01359}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the complex I 49 kDa
CC subunit family. {ECO:0000256|ARBA:ARBA00010019, ECO:0000256|HAMAP-
CC Rule:MF_01359}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the complex I 30 kDa
CC subunit family. {ECO:0000256|HAMAP-Rule:MF_01359}.
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DR EMBL; DS999411; EED34779.1; -; Genomic_DNA.
DR AlphaFoldDB; B8KTH8; -.
DR STRING; 565045.NOR51B_718; -.
DR eggNOG; COG0649; Bacteria.
DR HOGENOM; CLU_015134_3_2_6; -.
DR Proteomes; UP000004699; Unassembled WGS sequence.
DR GO; GO:0030964; C:NADH dehydrogenase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
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; IPR020396; NADH_UbQ_OxRdtase_CS.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR NCBIfam; TIGR01961; NuoC_fam; 1.
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; PS00542; COMPLEX1_30K; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01359};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01359};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01359};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01359};
KW Oxidoreductase {ECO:0000313|EMBL:EED34779.1};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01359};
KW Reference proteome {ECO:0000313|Proteomes:UP000004699};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01359};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01359};
KW Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01359}.
FT DOMAIN 47..171
FT /note="NADH:ubiquinone oxidoreductase 30kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF00329"
FT DOMAIN 322..592
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
FT REGION 1..183
FT /note="NADH dehydrogenase I subunit C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01359"
FT REGION 207..592
FT /note="NADH dehydrogenase I subunit D"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01359"
SQ SEQUENCE 592 AA; 66825 MW; AE39A22308043A89 CRC64;
MRPDQPAGER MVNAVVTADS GALEELLATL PDAGMAQQIT ADGTPTVWVP RERLLDVLRH
LRPGFPMLLD VFGIDERLRQ NKPLPAQDFT VVYHLFSVER REEFRVKASV SEADAVVPSA
TPVWPAANWY EREAWDMFGI EFSGHPNLRR IILPPTWEGF ALRKDHPARA TEMEPFSLDE
DKQVVEQEAL RFRPEEWGMD RASDDSEFMF LNLGPNHPSV HGVFRIALQL DGEVIVDAVP
DIGYHHRGAE KMGERQSWHT FIPYTDRIDY LGGVMNNLAY VLSVEKLAGI EVPPRVKVIR
IMLAELFRIS SHLVFYGTFV QDVGQMSPVF YMFADRERLF GIVEAITGGR MHPAWFRIGG
VAQDLPKGWD TLVRDFIDSM PARLDHYQKM AMDNSIVKDR TVGIGAYSGE EAVEWGITGA
SLRAAGVDFD LRRDRPYAGY EDFDFEVPLG HRGDSYDRAV VRVEEIRQSL RIIRQCLDNM
PEGPYKSDHR HTTPPPKERT LGDIETLIHH FLNVSWGPAI PPGEACVPIE ATKGFNSYHL
VSDGGTSSYR TRIRTPSFPA LQQLPLISRG LLIPDLIAII ASIDFVMADV DR
//
