NU4C_PROM1
ID NU4C_PROM1 Reviewed; 538 AA.
AC A2BZX6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=NAD(P)H-quinone oxidoreductase chain 4 {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 {ECO:0000255|HAMAP-Rule:MF_00491};
DE AltName: Full=NDH-1, chain 4 {ECO:0000255|HAMAP-Rule:MF_00491};
GN Name=ndhD {ECO:0000255|HAMAP-Rule:MF_00491}; OrderedLocusNames=NATL1_02221;
OS Prochlorococcus marinus (strain NATL1A).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167555;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL1A;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000553; ABM74786.1; -; Genomic_DNA.
DR RefSeq; WP_011823010.1; NC_008819.1.
DR AlphaFoldDB; A2BZX6; -.
DR SMR; A2BZX6; -.
DR STRING; 167555.NATL1_02221; -.
DR EnsemblBacteria; ABM74786; ABM74786; NATL1_02221.
DR KEGG; pme:NATL1_02221; -.
DR eggNOG; COG1008; Bacteria.
DR HOGENOM; CLU_007100_4_0_3; -.
DR OMA; ITRWGNQ; -.
DR Proteomes; UP000002592; 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..538
FT /note="NAD(P)H-quinone oxidoreductase chain 4"
FT /id="PRO_0000343242"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 285..305
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 340..360
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 382..404
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
SQ SEQUENCE 538 AA; 58755 MW; 341BE186873E3BD6 CRC64;
MLIPEPIQAD FPWLSLSILF PIVGALIVPF IPDKGEGKEV RWYALIISLI TFLITVAAYF
KGFDPSLEGL QLYEKVSWLP DLGLTWSVGA DGLSMPLILL TSFITSLAVL AAWPVSYKPK
LFFFLILAMD GGQIAVFAVQ DMLLFFLAWE LELFPVYLFL AIWGGKKRQY AATKFIIYTA
GSSLFILLAG LAMGFFQGGG VPDFGYTHLA QQNFGRGFQL LCYSGLLIAF GVKLPIVPLH
TWLPDAHGEA TAPVHMLLAG ILLKMGGYAL LRFNAQLLPD AHAQFAPLLI VLGVVNIIYA
ALTSFAQRNL KRKIAYSSIS HMGFVLIGIG SFSSLGTSGA MLQMVSHGLI GASLFFLVGA
TYDRTHTLQL DEMGGIGQNM RIMFALWTAC AFASLALPGM SGFISELMVF VGFVTDEVYT
LPFRIVVASL AAIGVILTPI YLLSMLREIF FGKENAKLIS KAKLVDAEPR EIYIIACLLV
PIIGIGLYPK IMTDTYISSI DGLVKRDLLA VERIRSDRAT IMSNTSLSIG TIEAPLLD
