ID A0A220XL28_ZANAE Unreviewed; 158 AA. AC A0A220XL28; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 11-DEC-2019, entry version 23. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit J, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01357}; DE EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01357}; DE AltName: Full=NAD(P)H dehydrogenase, subunit J {ECO:0000256|HAMAP-Rule:MF_01357}; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit J {ECO:0000256|HAMAP-Rule:MF_01357}; GN Name=ndhJ {ECO:0000256|HAMAP-Rule:MF_01357, GN ECO:0000313|EMBL:ASL06289.1}; OS Zantedeschia aethiopica (White calla lily) (Calla aethiopica). OG Plastid; Chloroplast {ECO:0000313|EMBL:ASL06289.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Philodendroideae; OC Zantedeschieae; Zantedeschia. OX NCBI_TaxID=69721 {ECO:0000313|EMBL:ASL06289.1}; RN [1] {ECO:0000313|EMBL:ASL06289.1} RP NUCLEOTIDE SEQUENCE. RA Tian N., Han L., Wang Z.; RT "The complete chloroplast genome sequence of Zantedeschia aethiopica."; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. 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_01357, ECO:0000256|RuleBase:RU003581, CC ECO:0000256|SAAS:SAAS01103434}. 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_01357, CC ECO:0000256|RuleBase:RU003581}; 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_01357, CC ECO:0000256|RuleBase:RU003581}; 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_01357, CC ECO:0000256|RuleBase:RU003581, ECO:0000256|SAAS:SAAS01103425}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003581, CC ECO:0000256|SAAS:SAAS01103439}; Peripheral membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003581, CC ECO:0000256|SAAS:SAAS01103439}; Stromal side {ECO:0000256|HAMAP- CC Rule:MF_01357, ECO:0000256|RuleBase:RU003581, CC ECO:0000256|SAAS:SAAS01103439}. CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family. CC {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003581}. 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; KY792991; ASL06289.1; -; Genomic_DNA. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-UniRule. DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.460.80; -; 1. DR HAMAP; MF_01357; NDH1_NuoC; 1. DR InterPro; IPR010218; NADH_DH_suC. DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like. DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su. DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS. DR Pfam; PF00329; Complex1_30kDa; 1. DR SUPFAM; SSF143243; SSF143243; 1. DR PROSITE; PS00542; COMPLEX1_30K; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000256|RuleBase:RU003581, ECO:0000256|SAAS:SAAS01103429, KW ECO:0000313|EMBL:ASL06289.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003581}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003581}; KW NADP {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003581, KW ECO:0000256|SAAS:SAAS01119003}; KW Plastid {ECO:0000256|RuleBase:RU003581, ECO:0000313|EMBL:ASL06289.1}; KW Plastoquinone {ECO:0000256|HAMAP-Rule:MF_01357, KW ECO:0000256|RuleBase:RU003581, ECO:0000256|SAAS:SAAS01119008}; KW Quinone {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003581}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003581, KW ECO:0000256|SAAS:SAAS01119018}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01357, KW ECO:0000256|RuleBase:RU003581}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01357, ECO:0000256|RuleBase:RU003581}. FT DOMAIN 30..148 FT /note="Complex1_30kDa" FT /evidence="ECO:0000259|Pfam:PF00329" SQ SEQUENCE 158 AA; 18580 MW; A242B976F38645CA CRC64; MQSHLSAWLI KHELVHRSLG FDYQGIETLQ IKSEDWDSIA VISYVYGYNY LRSQCAYDVA PGGFLASVYH LTRIQYGVDQ PEEVCIKVFA PRKNPGIPSV FWVWRSADFQ ERESYDMLGI SYDNHPRLKR ILMPESWIGW PLRKDYITPN FYEIQDAH //