ID NU5C_AGRST Reviewed; 739 AA. AC A1EA56; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 13-SEP-2023, entry version 58. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic; DE EC=7.1.1.-; DE AltName: Full=NAD(P)H dehydrogenase subunit 5; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 5; GN Name=ndhF; OS Agrostis stolonifera (Creeping bentgrass). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Pooideae; Poodae; Poeae; Poeae Chloroplast Group 1 (Aveneae type); OC Agrostidodinae; Agrostidinae; Agrostis. OX NCBI_TaxID=63632; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Penn A-4; RX PubMed=17534593; DOI=10.1007/s00122-007-0567-4; RA Saski C., Lee S.-B., Fjellheim S., Guda C., Jansen R.K., Luo H., RA Tomkins J., Rognli O.A., Daniell H., Clarke J.L.; RT "Complete chloroplast genome sequences of Hordeum vulgare, Sorghum bicolor RT and Agrostis stolonifera, and comparative analyses with other grass RT genomes."; RL Theor. Appl. Genet. 115:571-590(2007). CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN CC and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain CC and possibly in a chloroplast respiratory chain. The immediate electron CC acceptor for the enzyme in this species is believed to be CC plastoquinone. Couples the redox reaction to proton translocation, and CC thus conserves the redox energy in a proton gradient (By similarity). CC {ECO:0000250}. 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 -!- 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 -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which CC are encoded in the nucleus. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EF115543; ABK79628.1; -; Genomic_DNA. DR RefSeq; YP_874784.1; NC_008591.1. DR AlphaFoldDB; A1EA56; -. DR SMR; A1EA56; -. DR GeneID; 4525032; -. DR GO; GO:0009535; C:chloroplast 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 Gene3D; 1.20.5.2700; -; 1. DR InterPro; IPR002128; NADH_UbQ_OxRdtase_chlpt_su5_C. DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr. DR InterPro; IPR001750; ND/Mrp_mem. DR InterPro; IPR003945; NU5C-like. DR InterPro; IPR001516; Proton_antipo_N. DR NCBIfam; TIGR01974; NDH_I_L; 1. DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1. DR PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1. DR Pfam; PF01010; Proton_antipo_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. DR PRINTS; PR01434; NADHDHGNASE5. DR PRINTS; PR01435; NPOXDRDTASE5. PE 3: Inferred from homology; KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone; KW Thylakoid; Translocase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..739 FT /note="NAD(P)H-quinone oxidoreductase subunit 5, FT chloroplastic" FT /id="PRO_0000360908" FT TRANSMEM 9..29 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 39..59 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 89..109 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 125..145 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 147..167 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 185..205 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 219..239 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 258..278 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 280..300 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 327..347 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 354..374 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 396..416 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 425..445 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 542..562 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 610..630 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 719..739 FT /note="Helical" FT /evidence="ECO:0000255" SQ SEQUENCE 739 AA; 82746 MW; 0FB9FC89321D7ABF CRC64; MEHTYQYAWV IPLLPLPVIM SMGFGLFFIP TATKNLRRIW AFPSVLLLSI AMVFSVQLSI QQINGSSIYQ YLWSWTVNND FSLEFGYLID PLTSIMLILI TTVGILVLIY SDGYMSHDEG YLRFFVYISF FNTSMLGLVT SSNLIQIYFF WELVGMCSYL LIGFWFTRPL AASACQKAFV TNRVGDFGLL LGILGFFWIT GSLEFRDLFK IANNWIPNNG INSLLTTLCA FLLFLGAVAK SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLLARL LPLFISLPLI MSLISLVGTI TLFLGATLAL AQRDIKRSLA YSTMSQLGYM MLALGIGSYQ AALFHLITHA YSKALLFLGS GSIIHSMEPL VGYSPDKSQN MVLMGGLRKY IPITRSTFLW GTLSLCGIPP LACFWSKDEI LSNSWLYSPF FGIIASFTAG LTAFYMFRIY LLTFDGYLRV HFQNYSSTKE GPLYSISLWG KRIPKGVNGD FVLSTTKSGV SFFSQNIPKM QGNTTNRIGC FSTSFGAKKT FAYPHETGNT MLFPLLILLL FTFFIGFIGI SFDNGATDNG IAGLTILSKW LTPSINFTQE SSNSSINSYE FITNAISSVS LAIFGLFIAY IFYGSAYSFF QNLDLQNSFY KESPKKAFFG KVKKKIYSWS YNRGYIDIFY TRVFTLGIRG LTELTEFFDK GVIDGITNGV GLVSFCIGEE IKYVGGGRIS SYLFFFLCYV SIFLFFFLF //