ID A0A1I4AHY6_9PROT Unreviewed; 570 AA.
AC A0A1I4AHY6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|HAMAP-Rule:MF_01358};
DE Includes:
DE RecName: Full=NADH-quinone oxidoreductase subunit C {ECO:0000256|HAMAP-Rule:MF_01357};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01357};
DE AltName: Full=NADH dehydrogenase I subunit C {ECO:0000256|HAMAP-Rule:MF_01357};
DE AltName: Full=NDH-1 subunit C {ECO:0000256|HAMAP-Rule:MF_01357};
DE Includes:
DE RecName: Full=NADH-quinone oxidoreductase subunit D {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 Synonyms=nuoC {ECO:0000256|HAMAP-Rule:MF_01357};
GN ORFNames=SAMN05216302_100928 {ECO:0000313|EMBL:SFK55627.1};
OS Nitrosomonas aestuarii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=52441 {ECO:0000313|EMBL:SFK55627.1, ECO:0000313|Proteomes:UP000199533};
RN [1] {ECO:0000313|Proteomes:UP000199533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm69 {ECO:0000313|Proteomes:UP000199533};
RA Varghese N., Submissions S.;
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 ECO:0000256|HAMAP-Rule:MF_01357}.
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_01357};
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_01357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01357};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01357};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01357}.
CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01357}.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01358}.
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; FOSP01000009; SFK55627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4AHY6; -.
DR STRING; 52441.SAMN05216302_100928; -.
DR OrthoDB; 9801496at2; -.
DR Proteomes; UP000199533; 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: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_01358; NDH1_NuoD; 1.
DR InterPro; IPR010218; NADH_DH_suC.
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; 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; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01357};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01357};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01357};
KW Quinone {ECO:0000256|HAMAP-Rule:MF_01357};
KW Reference proteome {ECO:0000313|Proteomes:UP000199533};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01357};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01357};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|HAMAP-
KW Rule:MF_01357}.
FT DOMAIN 32..152
FT /note="NADH:ubiquinone oxidoreductase 30kDa subunit"
FT /evidence="ECO:0000259|Pfam:PF00329"
FT DOMAIN 300..570
FT /note="NADH-quinone oxidoreductase subunit D"
FT /evidence="ECO:0000259|Pfam:PF00346"
SQ SEQUENCE 570 AA; 64862 MW; 343C4EC4A2A8417C CRC64;
MTDGKMTLST QLETRFNATS CELSHDRIKT LSVPLERVTE TLEFLKYEAT PHFEMLFDLS
AIDETERNGG LTVFYQLLSL SGNADLRIKV NLPAKNPVLP SICSVWRAAN WYERELYDMF
GIHVDNHPNL VRILMPEYWE GHPLRKGHPN RATDMPPYQL PEAHYREIME SYRAEDYREP
MDDTEELTLN IGPTHPGTHG LLRLVVRLKG EEIRDVRPDI GFHHRGAEKM AERQTFHSYI
PYTDRIDYLS GVQNELPYLL AVEQLAGITV PERAQVIRVM LCELFRISSH LVWLASYSHD
LGALAPPFYA FRDREYLFDA IELITGGRMH PAFFRIGGVA MDLPEGWHEA IQAFLKRMLA
AIDEYQALLT HNPIMRARTR GIGILSVTEA IDWGVSGPNL RACGLAWDLR KCRPYSGYEQ
YDFEIPTAIK GDSLARAEVR LEEIRQSLRI VEQAIQNMPN GAVLSDQARY AFARKEATLQ
DIETLIHHFI TVGQGMTFPS GESLFITEAP KGMNGYFVVS NGTEHPYRLR IRTPSFPHMQ
ALAPLATGHL LADLIAILGS IDYILADIDR
//
