NDHI_ANTAG
ID NDHI_ANTAG Reviewed; 183 AA.
AC Q85A84;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit I, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01351};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01351};
DE AltName: Full=NAD(P)H dehydrogenase subunit I {ECO:0000255|HAMAP-Rule:MF_01351};
DE Short=NDH subunit I {ECO:0000255|HAMAP-Rule:MF_01351};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit I {ECO:0000255|HAMAP-Rule:MF_01351};
GN Name=ndhI {ECO:0000255|HAMAP-Rule:MF_01351};
OS Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC Anthoceros.
OX NCBI_TaxID=48387;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=12527781; DOI=10.1093/nar/gkg155;
RA Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT chloroplast genome: insight into the earliest land plants.";
RL Nucleic Acids Res. 31:716-721(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=12711687; DOI=10.1093/nar/gkg327;
RA Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT "RNA editing in hornwort chloroplasts makes more than half the genes
RT functional.";
RL Nucleic Acids Res. 31:2417-2423(2003).
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:0000255|HAMAP-Rule:MF_01351}.
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_01351};
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_01351};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01351};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01351};
CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC are encoded in the nucleus. {ECO:0000255|HAMAP-Rule:MF_01351}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01351}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01351}.
CC -!- RNA EDITING: Modified_positions=30 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 52 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 132 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 135 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 139 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 142 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}; Note=The nonsense codons in positions 52
CC and 139 are modified to sense codons.;
CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01351}.
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DR EMBL; AB086179; BAC55405.1; -; Genomic_DNA.
DR EMBL; AB087489; BAC55505.1; -; mRNA.
DR RefSeq; NP_777468.1; NC_004543.1.
DR AlphaFoldDB; Q85A84; -.
DR SMR; Q85A84; -.
DR GeneID; 2553502; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01351; NDH1_NuoI; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004497; NADH_plast_OxRdtase_su_I.
DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR PANTHER; PTHR47275; PTHR47275; 1.
DR Pfam; PF13237; Fer4_10; 1.
DR TIGRFAMs; TIGR00403; ndhI; 1.
DR TIGRFAMs; TIGR01971; NuoI; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Chloroplast; Iron; Iron-sulfur; Membrane; Metal-binding; NAD; NADP;
KW Plastid; Plastoquinone; Quinone; Repeat; RNA editing; Thylakoid;
KW Translocase.
FT CHAIN 1..183
FT /note="NAD(P)H-quinone oxidoreductase subunit I,
FT chloroplastic"
FT /id="PRO_0000118703"
FT DOMAIN 55..84
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT DOMAIN 95..124
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 74
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 104
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 107
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
SQ SEQUENCE 183 AA; 21437 MW; DDF8A4B593609E0F CRC64;
MFSMVNGFRN YSQQAIQASR YIGQGFIVTL DHMNRLPMTI QYPYEKLVPS ERFRGRIHFE
FDKCIACEVC VRVCPINLPV VDWKFKKDIK KKQLKSYSID FGVCIFCGNC VEYCPTNCLS
MTEEYELSTY DRHELNYDQI ALGRLPISII EDRTIESISS FDFSSKKIME EHSKSRTVTK
FLD
