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Database: UniProt
Entry: K9Z774_CYAAP
LinkDB: K9Z774_CYAAP
Original site: K9Z774_CYAAP 
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
//
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