NDHI_THEVB
ID NDHI_THEVB Reviewed; 196 AA.
AC Q8DL31;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit I {ECO:0000255|HAMAP-Rule:MF_01351};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01351};
DE AltName: Full=NAD(P)H dehydrogenase I subunit I {ECO:0000255|HAMAP-Rule:MF_01351};
DE AltName: Full=NDH-1 subunit I {ECO:0000255|HAMAP-Rule:MF_01351};
DE Short=NDH-I {ECO:0000255|HAMAP-Rule:MF_01351};
GN Name=ndhI {ECO:0000255|HAMAP-Rule:MF_01351}; OrderedLocusNames=tlr0668;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
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. {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-1 is composed of at least 11 different subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01351}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01351}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01351}.
CC -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01351}.
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DR EMBL; BA000039; BAC08219.1; -; Genomic_DNA.
DR RefSeq; NP_681457.1; NC_004113.1.
DR RefSeq; WP_011056515.1; NC_004113.1.
DR PDB; 6HUM; EM; 3.34 A; I=1-196.
DR PDB; 6KHI; EM; 3.00 A; I=1-196.
DR PDB; 6KHJ; EM; 3.00 A; I=1-196.
DR PDB; 6L7O; EM; 3.20 A; I=1-196.
DR PDB; 6L7P; EM; 3.60 A; I=1-196.
DR PDB; 6NBQ; EM; 3.10 A; I=1-196.
DR PDB; 6NBX; EM; 3.50 A; I=1-196.
DR PDB; 6NBY; EM; 3.10 A; I=1-196.
DR PDB; 6TJV; EM; 3.20 A; I=1-196.
DR PDBsum; 6HUM; -.
DR PDBsum; 6KHI; -.
DR PDBsum; 6KHJ; -.
DR PDBsum; 6L7O; -.
DR PDBsum; 6L7P; -.
DR PDBsum; 6NBQ; -.
DR PDBsum; 6NBX; -.
DR PDBsum; 6NBY; -.
DR PDBsum; 6TJV; -.
DR AlphaFoldDB; Q8DL31; -.
DR SMR; Q8DL31; -.
DR IntAct; Q8DL31; 1.
DR STRING; 197221.22294389; -.
DR TCDB; 3.D.1.8.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAC08219; BAC08219; BAC08219.
DR KEGG; tel:tlr0668; -.
DR PATRIC; fig|197221.4.peg.707; -.
DR eggNOG; COG1143; Bacteria.
DR OMA; PVVDWVM; -.
DR OrthoDB; 1619561at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived 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; PF12838; Fer4_7; 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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Iron; Iron-sulfur; Membrane; Metal-binding; NAD;
KW NADP; Plastoquinone; Quinone; Reference proteome; Repeat; Thylakoid;
KW Translocase.
FT CHAIN 1..196
FT /note="NAD(P)H-quinone oxidoreductase subunit I"
FT /id="PRO_0000245687"
FT DOMAIN 54..83
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT DOMAIN 94..123
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT REGION 174..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63
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 66
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 69
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 73
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 103
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 106
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 109
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 113
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01351"
FT HELIX 4..29
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6NBQ"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6NBY"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6NBQ"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:6KHJ"
FT TURN 138..142
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:6KHJ"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:6NBQ"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6NBQ"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6KHJ"
FT HELIX 184..192
FT /evidence="ECO:0007829|PDB:6KHI"
SQ SEQUENCE 196 AA; 22416 MW; C0E4ED55F3DFC670 CRC64;
MKFLNQITNY AKEAVQSAKY IGQGLSVTFD HMRRRPITVQ YPYEKLIPSE RFRGRIHFEF
DKCIACEVCV RVCPINLPVV DWVFNKELKK KELKHYSIDF GVCIFCANCV EYCPTNCLSV
TEEYELATYD RHELNYDSVA MGRIPYKVTQ DPMVTPIREF AYLPAGVMSG HDLPAGAQRA
GERPEAIANT AKSSEN
