ID H6CSQ7_ORYRU Unreviewed; 510 AA.
AC H6CSQ7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic {ECO:0000256|HAMAP-Rule:MF_00445};
DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_00445};
DE AltName: Full=NAD(P)H dehydrogenase, subunit 2 {ECO:0000256|HAMAP-Rule:MF_00445};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 2 {ECO:0000256|HAMAP-Rule:MF_00445};
GN Name=ndhB {ECO:0000256|HAMAP-Rule:MF_00445,
GN ECO:0000313|EMBL:AEI53148.1};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OG Plastid; Chloroplast {ECO:0000313|EMBL:AEI53148.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EMBL:AEI53148.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|EMBL:AEI53148.1, ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1943 {ECO:0000313|Proteomes:UP000008022};
RX PubMed=22408737; DOI=10.1002/ece3.66;
RA Waters D.L.E., Nock C.J., Rice N., Ishikawa R., Henry R.J.;
RT "Chloroplast genome sequence confirms distinctness of Australian and Asian
RT wild rice.";
RL Ecol. Evol. 2:211-217(2012).
RN [2] {ECO:0000313|EMBL:AGY93240.1}
RP NUCLEOTIDE SEQUENCE.
RA Pilkington S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AGZ19257.1}
RP NUCLEOTIDE SEQUENCE.
RA Lin Z., Fan L.;
RT "The chloroplast genome of Chinese wild rice (Dongxiang).";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AGY48994.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25329378;
RA Brozynska M., Furtado A., Henry R.J.;
RT "Direct chloroplast sequencing: comparison of sequencing platforms and
RT analysis tools for whole chloroplast barcoding.";
RL PLoS ONE 9:E110387-E110387(2014).
RN [5] {ECO:0000313|EMBL:AJC09687.1}
RP NUCLEOTIDE SEQUENCE.
RA Chen X.-L., Norrbom A., Zhu C.-D.;
RT "A systematic study of Ichneumonosoma Meijere, Pelmatops Enderlein,
RT Pseudopelmatops Shiraki and Soita Walker (Diptera: Tephritidae).";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:QTW91050.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Or135 {ECO:0000313|EMBL:QTW91050.1}, and Or136
RC {ECO:0000313|EMBL:QTW91136.1};
RA Li T.-Z.;
RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) that is believed to belong to the
CC minimal assembly required for catalysis. Complex I functions in the
CC transfer of electrons from NADH to the respiratory chain. The immediate
CC electron acceptor for the enzyme is believed to be ubiquinone.
CC {ECO:0000256|ARBA:ARBA00003257}.
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.
CC {ECO:0000256|HAMAP-Rule:MF_00445}.
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_00445};
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_00445};
CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC are encoded in the nucleus. {ECO:0000256|HAMAP-Rule:MF_00445}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid,
CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_00445};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00445}.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000256|HAMAP-Rule:MF_00445}.
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DR EMBL; JN005832; AEI53130.1; -; Genomic_DNA.
DR EMBL; JN005832; AEI53148.1; -; Genomic_DNA.
DR EMBL; JN005833; AEI53207.1; -; Genomic_DNA.
DR EMBL; JN005833; AEI53223.1; -; Genomic_DNA.
DR EMBL; KF428978; AGY48994.1; -; Genomic_DNA.
DR EMBL; KF428978; AGY49028.1; -; Genomic_DNA.
DR EMBL; KF359902; AGY93240.1; -; Genomic_DNA.
DR EMBL; KF359902; AGY93259.1; -; Genomic_DNA.
DR EMBL; KF562709; AGZ19257.1; -; Genomic_DNA.
DR EMBL; KF562709; AGZ19280.1; -; Genomic_DNA.
DR EMBL; KM103372; AJC09687.1; -; Genomic_DNA.
DR EMBL; KM103372; AJC09709.1; -; Genomic_DNA.
DR EMBL; MW711321; QTW91050.1; -; Genomic_DNA.
DR EMBL; MW711321; QTW91067.1; -; Genomic_DNA.
DR EMBL; MW711322; QTW91136.1; -; Genomic_DNA.
DR EMBL; MW711322; QTW91153.1; -; Genomic_DNA.
DR RefSeq; YP_006280798.1; NC_017835.1.
DR RefSeq; YP_006280816.1; NC_017835.1.
DR AlphaFoldDB; H6CSQ7; -.
DR SMR; H6CSQ7; -.
DR STRING; 4529.H6CSQ7; -.
DR GeneID; 12486670; -.
DR GeneID; 12486697; -.
DR Proteomes; UP000008022; Chloroplast.
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 GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR045693; Ndh2_N.
DR NCBIfam; TIGR01770; NDH_I_N; 1.
DR PANTHER; PTHR22773:SF112; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 2 B, CHLOROPLASTIC; 1.
DR PANTHER; PTHR22773; NADH DEHYDROGENASE; 1.
DR Pfam; PF19530; Ndh2_N; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01434; NADHDHGNASE5.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000313|EMBL:AEI53148.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00445};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00445};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00445};
KW Oxidoreductase {ECO:0000313|EMBL:AGY48994.1};
KW Plastid {ECO:0000313|EMBL:AEI53148.1};
KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957, ECO:0000256|HAMAP-
KW Rule:MF_00445};
KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_00445};
KW Reference proteome {ECO:0000313|Proteomes:UP000008022};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_00445};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_00445};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00445};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00445};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00445}.
FT TRANSMEM 22..47
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 126..143
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 181..203
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 223..242
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 295..316
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 323..342
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 348..372
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 393..415
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT TRANSMEM 427..448
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT DOMAIN 18..117
FT /note="NAD(P)H-quinone oxidoreductase subunit 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19530"
FT DOMAIN 146..443
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
SQ SEQUENCE 510 AA; 56769 MW; 8BC27F90806815E6 CRC64;
MIWHVQNENF ILDSTRIFMK AFHLLLFQGS FIFPECILIF GLILLLMIDL TSDQKDRPWF
YFISSTSLVI SITALLFRWR EEPIISFSGN FQTNNFNEIF QFLILLCSTL CIPLSVEYIE
CTEMAITEFL LFVLTATLGG MFLCGANDLI TIFVAPECFS LCSYLLSGYT KRDLRSNEAT
MKYLLMGGAS SSILVHGFSW LYGSSGGEIE LQEIVNGLIN TQMYNSPGIS IALISITVGL
GFKLSPAPFH QWTPDVYEGS PTPVVAFLSV TSKVAASASA TRILDIPFYF SSNEWHLLLE
ILAILSMILG NLLAITQTSM KRMLAYSSIG QIGYVIIGII VGDSNDGYAS MITYMLFYIS
MNLGTFACIV LFGLRTGTDN IRDYAGLYTK DPFLALSLAL CLLSLGGLPP LAGFFGKLYL
FWCGWQAGLY FLVSIGLLTS VLSIYYYLKI VKLLMTGRNQ EITPYVRNYR RSPLRSNNSI
ELSMTVCVIA STIPGISMNP ILAIAQDTLF
//
