ID K9Z774_CYAAP Unreviewed; 606 AA.
AC K9Z774;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=NAD(P)H dehydrogenase, subunit NdhF3 family {ECO:0000313|EMBL:AFZ55051.1};
DE EC=1.6.5.11 {ECO:0000313|EMBL:AFZ55051.1};
GN OrderedLocusNames=Cyan10605_2991 {ECO:0000313|EMBL:AFZ55051.1};
OS Cyanobacterium aponinum (strain PCC 10605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Cyanobacterium.
OX NCBI_TaxID=755178 {ECO:0000313|EMBL:AFZ55051.1, ECO:0000313|Proteomes:UP000010480};
RN [1] {ECO:0000313|Proteomes:UP000010480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 10605 {ECO:0000313|Proteomes:UP000010480};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000320}.
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DR EMBL; CP003947; AFZ55051.1; -; Genomic_DNA.
DR RefSeq; WP_015220770.1; NC_019776.1.
DR AlphaFoldDB; K9Z774; -.
DR STRING; 755178.Cyan10605_2991; -.
DR KEGG; can:Cyan10605_2991; -.
DR PATRIC; fig|755178.3.peg.3186; -.
DR eggNOG; COG1009; Bacteria.
DR HOGENOM; CLU_007100_6_3_3; -.
DR OMA; MDWGWAR; -.
DR OrthoDB; 9807568at2; -.
DR Proteomes; UP000010480; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR Gene3D; 1.20.5.2700; -; 1.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR003945; NU5C-like.
DR InterPro; IPR010217; NU5C2.
DR InterPro; IPR001516; Proton_antipo_N.
DR NCBIfam; TIGR01960; ndhF3_CO2; 1.
DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR Pfam; PF00662; Proton_antipo_N; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:AFZ55051.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010480};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000320};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 38..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 413..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 485..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 585..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..122
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 139..399
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 606 AA; 66549 MW; 0EBD16A725341917 CRC64;
MNFFSETIWF IPCYTLIGGL IALLWSPGII RKTGSRPAGY VNIVMTSLAF IHSVVALYQI
WEKPAQEFRF TWLEAAGVNI SFDLQISSVS VGALALITGL NVLSQIYAIG YLEMDWGWAR
FYALMGFFEA GMCGLVLCNS LFFSYVYLEI LTLGTYLLVG FWFAQPLVVS GARDAFWTKR
VGDILLLMGV IAIYPFSNTW NYNYLAFWAE NSPIDNTFST LLCLALISGP IAKCAQIPLQ
LWLDEAMEGP LPASILRNAI VVTVGAYVII QLQPVLAMSP IASQAVTIIG VITAILASLI
SIAQVDIKRV LSYLVSAYMG LVFIAVGTNH EKTALVLIAV YAVAMALLYM SIGAIIISNI
TQDLTQLGGL WKKRPLAGIA FLVGSFGLVA FPPLGGFWIL PQLGNDFFVS QPWLVGVLLI
VDALTAFSLL RTFCLIFLGD SKQMTVRSPE VLWAMVLPMM ILTGVTLHLP LVLAQFNLIS
FQGNLNIFFS VSTLIGVVLA MLIYGKKPAD KSVDVVPEFV RNFFANDLYI QDIYKVTVVG
IVNVTAKLAY WFDRYIVDGV VNLVGLSTIF GGQALKYSTS GQSQLYIFSI LLGLIFVAII
FGLTQF
//