NU4C1_TRIV2
ID NU4C1_TRIV2 Reviewed; 525 AA.
AC Q3MCB9;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=NAD(P)H-quinone oxidoreductase chain 4 1 {ECO:0000255|HAMAP-Rule:MF_00491};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00491};
DE AltName: Full=NAD(P)H dehydrogenase I, chain 4 1 {ECO:0000255|HAMAP-Rule:MF_00491};
DE AltName: Full=NDH-1, chain 4 1 {ECO:0000255|HAMAP-Rule:MF_00491};
GN Name=ndhD1 {ECO:0000255|HAMAP-Rule:MF_00491}; OrderedLocusNames=Ava_1745;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
CC -!- FUNCTION: NDH-1 shuttles electrons from NAD(P)H, via FMN and iron-
CC sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC immediate electron acceptor for the enzyme in this species is believed
CC to be plastoquinone. Couples the redox reaction to proton translocation
CC (for every two electrons transferred, four hydrogen ions are
CC translocated across the cytoplasmic membrane), and thus conserves the
CC redox energy in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_00491}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00491};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00491};
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00491}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00491}.
CC -!- SIMILARITY: Belongs to the complex I subunit 4 family.
CC {ECO:0000255|HAMAP-Rule:MF_00491}.
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DR EMBL; CP000117; ABA21367.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3MCB9; -.
DR SMR; Q3MCB9; -.
DR STRING; 240292.Ava_1745; -.
DR EnsemblBacteria; ABA21367; ABA21367; Ava_1745.
DR KEGG; ava:Ava_1745; -.
DR eggNOG; COG1008; Bacteria.
DR HOGENOM; CLU_007100_4_0_3; -.
DR OMA; ITRWGNQ; -.
DR Proteomes; UP000002533; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR HAMAP; MF_00491; NDH1_NuoM; 1.
DR InterPro; IPR022997; NADH_Q_OxRdtase_chain4.
DR InterPro; IPR010227; NADH_Q_OxRdtase_chainM/4.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR PANTHER; PTHR43507; PTHR43507; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
DR TIGRFAMs; TIGR01972; NDH_I_M; 1.
PE 3: Inferred from homology;
KW Membrane; NAD; NADP; Plastoquinone; Quinone; Thylakoid; Translocase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..525
FT /note="NAD(P)H-quinone oxidoreductase chain 4 1"
FT /id="PRO_0000343230"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 375..397
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
SQ SEQUENCE 525 AA; 57613 MW; BCF32B4056858AAF CRC64;
MNTANFPWLT TIILLPIAAS LLIPIIPDKD GKTIRWYALI VGLIDFALIV YAFYTSYDFA
NPDLQLVESY PWVPQLDLNW SVGADGLSMP LIILTGFITT LATLAAWPVT LKPRLFYFLL
LAMYGGQIAV FAVQDLLLFF LVWELELIPV YLLLAIWGGK KRQYAATKFI LYTAGGSLFI
LLAALTMAFY GDNVTFDMRS LALKDYALNF QLLLYAGFLI AYAIKLPIIP LHTWLPDAHG
EATAPAHMLL AGILLKMGGY ALIRMNAGIL PDAHAYFAPV LVVLGVVNII YAALTSFAQR
NLKRKIAYSS ISHMGFVIIG FASFTDLGLS GAVLQMVSHG LIGASLFFLV GATYDRTHTL
MLDEMGGVGK RMPKIFAMFT ACSMASLALP GMSGFVAELM VFVGFATSDA YSSTFKVIVV
FLMAVGVILT PIYLLSMLRE IFYGKENEEL VSHQQLIDAE PREVFVIACL LVPIIGIGFY
PKLLTQMYDA TTVQLTARLR DSVPTLAQEK PEAPKVSLSA PVIGN
