NU4C_SYNSC
ID NU4C_SYNSC Reviewed; 533 AA.
AC Q3AGZ9;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
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};
GN OrderedLocusNames=Syncc9605_2401;
OS Synechococcus sp. (strain CC9605).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=110662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9605;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9605.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000110; ABB36133.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3AGZ9; -.
DR SMR; Q3AGZ9; -.
DR STRING; 110662.Syncc9605_2401; -.
DR EnsemblBacteria; ABB36133; ABB36133; Syncc9605_2401.
DR KEGG; syd:Syncc9605_2401; -.
DR eggNOG; COG1008; Bacteria.
DR HOGENOM; CLU_007100_4_0_3; -.
DR OMA; ITRWGNQ; -.
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..533
FT /note="NAD(P)H-quinone oxidoreductase chain 4"
FT /id="PRO_0000343253"
FT TRANSMEM 5..25
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 70..90
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 137..157
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 210..230
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00491"
SQ SEQUENCE 533 AA; 57310 MW; 0645348CABBAF0E2 CRC64;
MQATVPWLSL SILVPIVGAL LVPLVPDKGE GKQVRWYALI VTLITFLITV AAYLTGYDPS
LSGLQLSERV SWLPDLGLTW AVGADGLSMP LILLTSFITS LACLAAWPVS FKPRLFYFLL
LAMDGGQIAV FAVQDMLLFF LAWELELIPV YLLLAIWGGK KRQYAATKFI LYTAGSSLFI
LLAALAMGFF GGGTPSFEYT ALAAKDFGTG FQLLCYAGLL IAFGVKLPIV PLHTWLPDAH
GEATAPVHML LAGILLKMGG YALLRFNCEL LPAAHSQFAP LLIVLGVVNI IYAALTSFAQ
RNLKRKIAYS SISHMGFVLI GVGSFSALGT SGAMLQMISH GLIGASLFFL VGATYDRTHT
LQLDEMGGIG QKMRIMFALW TVCALASLAL PGMSGFVSEL MVFAGFATDE AYTLPFRVVI
CGLAAVGVIL TPIYLLSMLR EIFFGKEKEE LVSHTNLVDA EPREVYIIGC LLVPIIGIGL
YPKLMTDSYR SSIEALVSRN LGAMEQVISP TAPLIRGQAP VPAIIQAPAV GAS
