NDHJ_SYNY3
ID NDHJ_SYNY3 Reviewed; 179 AA.
AC P19125; P74194;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit J {ECO:0000255|HAMAP-Rule:MF_01357};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01357};
DE AltName: Full=NAD(P)H dehydrogenase subunit J;
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit J {ECO:0000255|HAMAP-Rule:MF_01357};
DE AltName: Full=NDH-1 subunit J {ECO:0000255|HAMAP-Rule:MF_01357};
DE Short=NDH-J {ECO:0000255|HAMAP-Rule:MF_01357};
DE AltName: Full=ORF 155;
GN Name=ndhJ {ECO:0000255|HAMAP-Rule:MF_01357}; OrderedLocusNames=slr1281;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2499764; DOI=10.1007/bf00332231;
RA Steinmueller K., Ley A.C., Steinmetz A.A., Sayre R.T., Bogorad L.;
RT "Characterization of the ndhC-psbG-ORF157/159 operon of maize plastid DNA
RT and of the cyanobacterium Synechocystis sp. PCC6803.";
RL Mol. Gen. Genet. 216:60-69(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP PROTEIN SEQUENCE OF 2-20 AND 23-40, AND CHARACTERIZATION AS A MEMBER OF THE
RP NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX.
RX PubMed=8325373; DOI=10.1016/0014-5793(93)81800-f;
RA Berger S., Ellersiek U., Kinzelt D., Steinmueller K.;
RT "Immunopurification of a subcomplex of the NAD(P)H-plastoquinone-
RT oxidoreductase from the cyanobacterium Synechocystis sp. PCC6803.";
RL FEBS Lett. 326:246-250(1993).
RN [4]
RP PROTEIN SEQUENCE OF 1-9, CHARACTERIZATION AS A MEMBER OF THE
RP NAD(P)H-QUINONE OXIDOREDUCTASE COMPLEX, AND SUBCOMPLEXES OF NDH-1.
RX PubMed=15102833; DOI=10.1074/jbc.m401107200;
RA Prommeenate P., Lennon A.M., Markert C., Hippler M., Nixon P.J.;
RT "Subunit composition of NDH-1 complexes of Synechocystis sp. PCC 6803:
RT identification of two new ndh gene products with nuclear-encoded homologues
RT in the chloroplast Ndh complex.";
RL J. Biol. Chem. 279:28165-28173(2004).
RN [5]
RP PROTEIN SEQUENCE OF 85-94; 109-126 AND 152-164, AND SUBCOMPLEXES OF NDH-1.
RX PubMed=15548534; DOI=10.1074/jbc.m410914200;
RA Battchikova N., Zhang P., Rudd S., Ogawa T., Aro E.-M.;
RT "Identification of NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes
RT of Synechocystis sp. PCC 6803.";
RL J. Biol. Chem. 280:2587-2595(2005).
RN [6]
RP SUBCELLULAR LOCATION IN THYLAKOID.
RX PubMed=16287171; DOI=10.1002/pmic.200500111;
RA Srivastava R., Pisareva T., Norling B.;
RT "Proteomic studies of the thylakoid membrane of Synechocystis sp. PCC
RT 6803.";
RL Proteomics 5:4905-4916(2005).
CC -!- FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via
CC FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory
CC and/or the photosynthetic chain. The immediate electron acceptor for
CC the enzyme in this species is believed to be plastoquinone. Couples the
CC redox reaction to proton translocation, and thus conserves the redox
CC energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in
CC inorganic carbon-concentration. {ECO:0000255|HAMAP-Rule:MF_01357}.
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:0000255|HAMAP-Rule:MF_01357};
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:0000255|HAMAP-Rule:MF_01357};
CC -!- SUBUNIT: NDH-1 can be composed of about 15 different subunits;
CC different subcomplexes with different compositions have been identified
CC which probably have different functions.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000305|PubMed:16287171}; Peripheral membrane protein
CC {ECO:0000305|PubMed:16287171}; Cytoplasmic side
CC {ECO:0000305|PubMed:16287171}.
CC -!- PTM: In at one experiment the initiator methionine has been seen to be
CC kept and removed. {ECO:0000269|PubMed:15102833}.
CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01357}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35486.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X17439; CAA35486.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000022; BAA18285.1; -; Genomic_DNA.
DR PIR; S75826; S75826.
DR AlphaFoldDB; P19125; -.
DR SMR; P19125; -.
DR IntAct; P19125; 11.
DR STRING; 1148.1653371; -.
DR PaxDb; P19125; -.
DR EnsemblBacteria; BAA18285; BAA18285; BAA18285.
DR KEGG; syn:slr1281; -.
DR eggNOG; COG0852; Bacteria.
DR InParanoid; P19125; -.
DR OMA; YELQDAY; -.
DR PhylomeDB; P19125; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived 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: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 1: Evidence at protein level;
KW Direct protein sequencing; Membrane; NAD; NADP; Plastoquinone; Quinone;
KW Reference proteome; Thylakoid; Translocase; Transport.
FT INIT_MET 1
FT /note="Removed; partial"
FT /evidence="ECO:0000269|PubMed:8325373"
FT CHAIN 2..179
FT /note="NAD(P)H-quinone oxidoreductase subunit J"
FT /id="PRO_0000118667"
SQ SEQUENCE 179 AA; 20593 MW; 3EE18D5E727F8BCC CRC64;
MAEEVNSPNE AVNLQEETAI APVGPVSTWL TTNGFEHQSL TADHLGVEMV QVEADLLLPL
CTALYAYGFN YLQCQGAYDE GPGKSLVSFY HLVKLTEDTR NPEEVRLKVF LPRENPVVPS
VYWIWKAADW QERECYDMFG IVYEGHPNLK RILMPEDWVG WPLRKDYISP DFYELQDAY
