ID K9V0Y3_9CYAN Unreviewed; 563 AA.
AC K9V0Y3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=NAD(P)H-quinone oxidoreductase chain 4 {ECO:0000256|HAMAP-Rule:MF_00491};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_00491};
DE AltName: Full=NAD(P)H dehydrogenase I, chain 4 {ECO:0000256|HAMAP-Rule:MF_00491};
DE AltName: Full=NDH-1, chain 4 {ECO:0000256|HAMAP-Rule:MF_00491};
GN Name=ndhD {ECO:0000256|HAMAP-Rule:MF_00491};
GN ORFNames=Cal6303_1876 {ECO:0000313|EMBL:AFZ00910.1};
OS Calothrix sp. PCC 6303.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ00910.1, ECO:0000313|Proteomes:UP000010477};
RN [1] {ECO:0000313|EMBL:AFZ00910.1, ECO:0000313|Proteomes:UP000010477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ00910.1,
RC ECO:0000313|Proteomes:UP000010477};
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL Submitted (MAY-2012) 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:0000256|ARBA:ARBA00025624,
CC ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00491};
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_00491}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00491}. Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}.
CC -!- SIMILARITY: Belongs to the complex I subunit 4 family.
CC {ECO:0000256|ARBA:ARBA00009025, ECO:0000256|HAMAP-Rule:MF_00491}.
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DR EMBL; CP003610; AFZ00910.1; -; Genomic_DNA.
DR RefSeq; WP_015197556.1; NC_019751.1.
DR AlphaFoldDB; K9V0Y3; -.
DR STRING; 1170562.Cal6303_1876; -.
DR KEGG; calt:Cal6303_1876; -.
DR PATRIC; fig|1170562.3.peg.2051; -.
DR eggNOG; COG1008; Bacteria.
DR HOGENOM; CLU_007100_4_0_3; -.
DR OrthoDB; 416973at2; -.
DR Proteomes; UP000010477; Chromosome.
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 NCBIfam; TIGR01972; NDH_I_M; 1.
DR PANTHER; PTHR43507:SF1; NAD(P)H-QUINONE OXIDOREDUCTASE CHAIN 4, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43507; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00491};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00491};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00491};
KW Oxidoreductase {ECO:0000313|EMBL:AFZ00910.1};
KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957, ECO:0000256|HAMAP-
KW Rule:MF_00491};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_00491};
KW Reference proteome {ECO:0000313|Proteomes:UP000010477};
KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00491};
KW Translocase {ECO:0000256|HAMAP-Rule:MF_00491};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00491,
KW ECO:0000256|RuleBase:RU000320};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00491}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 77..103
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 115..133
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 139..157
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 169..193
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 213..235
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 247..264
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 276..295
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 307..325
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 337..355
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 411..436
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT TRANSMEM 490..507
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00491"
FT DOMAIN 133..421
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 563 AA; 61591 MW; F998EA50E765D1A2 CRC64;
MMADQFPWLT AIILLPLVGA FLIPLLPDKD GKYVRWYALG VGIADFILMC LAFWLNYDPN
STTFQMAESY SWLPQIGLSW SVSVDGLSFP LVLLAGFVTT LAIFSAWQVD RRPKLFYSLM
LVLYAAQIGV FVAQDLLLFF IMWEVELIPV YLLICIWGGQ KRRYAATKFL IYTAAASIFI
IVAAIAMALY GGNDVTFDIV ALKLKDYPLG LELFLYAGLL IAFGVKLAVF PLHTWLPDAH
GEASSPVSMI LAGVLLKMGG YGIIRLNLEM LPNAHIYFAP VLAILGVVNI IYGALNSFAQ
NNMKRRLAYS SISHMGFVLL GIASFTDLGI NGAMLQMISH GLIASVLFFL AGITYDRTHT
MMMEEMGGVG QAMPKVFALF TIGAMASLAL PGMSGFAGEL SVFLGITTSD IYSSTFCTVT
IFLAAVGVIL TPIYLLNLLR QVFYGNGKSL ICDINNTTST NLTDEEVACF GTDCLLPSQS
IYRDASPREI FIAACFIVLI VGIGLYPKAA MGMYDAKTVA INTQVRQSYT QIAQTNPRVY
ANGFLNPQII ESEMPSVLGT LNQ
//
