NU2C_THEVB
ID NU2C_THEVB Reviewed; 515 AA.
AC Q8DMR6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00445};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NAD(P)H dehydrogenase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NDH-1, subunit 2 {ECO:0000255|HAMAP-Rule:MF_00445};
GN Name=ndhB {ECO:0000255|HAMAP-Rule:MF_00445}; OrderedLocusNames=tll0045;
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. Cyanobacterial NDH-1 also plays a role in
CC inorganic carbon-concentration. {ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00445};
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. {ECO:0000255|HAMAP-
CC Rule:MF_00445}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00445}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00445}.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
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DR EMBL; BA000039; BAC07598.1; -; Genomic_DNA.
DR RefSeq; NP_680836.1; NC_004113.1.
DR RefSeq; WP_011055900.1; NC_004113.1.
DR PDB; 6HUM; EM; 3.34 A; B=1-515.
DR PDB; 6KHI; EM; 3.00 A; B=1-515.
DR PDB; 6KHJ; EM; 3.00 A; B=1-515.
DR PDB; 6L7O; EM; 3.20 A; B=1-515.
DR PDB; 6L7P; EM; 3.60 A; B=1-515.
DR PDB; 6NBQ; EM; 3.10 A; B=1-515.
DR PDB; 6NBX; EM; 3.50 A; B=1-515.
DR PDB; 6NBY; EM; 3.10 A; B=1-515.
DR PDB; 6TJV; EM; 3.20 A; B=1-515.
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; Q8DMR6; -.
DR SMR; Q8DMR6; -.
DR IntAct; Q8DMR6; 1.
DR STRING; 197221.22293766; -.
DR TCDB; 3.D.1.8.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAC07598; BAC07598; BAC07598.
DR KEGG; tel:tll0045; -.
DR PATRIC; fig|197221.4.peg.44; -.
DR eggNOG; COG1007; Bacteria.
DR OMA; FYIRVIV; -.
DR OrthoDB; 1664448at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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 Pfam; PF19530; Ndh2_N; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR TIGRFAMs; TIGR01770; NDH_I_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; NAD; NADP; Plastoquinone; Quinone;
KW Reference proteome; Thylakoid; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..515
FT /note="NAD(P)H-quinone oxidoreductase subunit 2"
FT /id="PRO_0000225358"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 109..128
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 132..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 16..34
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 43..62
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6TJV"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 78..97
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 110..127
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 132..150
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 157..187
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 208..223
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 241..263
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 264..266
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 271..290
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 299..320
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 323..353
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 363..368
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 370..384
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:6TJV"
FT HELIX 390..403
FT /evidence="ECO:0007829|PDB:6KHI"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 408..433
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:6KHJ"
FT HELIX 442..445
FT /evidence="ECO:0007829|PDB:6KHI"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 457..476
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 479..486
FT /evidence="ECO:0007829|PDB:6KHI"
FT HELIX 488..491
FT /evidence="ECO:0007829|PDB:6NBQ"
SQ SEQUENCE 515 AA; 55144 MW; 24669A026C5620E8 CRC64;
MDLVTLAGQL NAGTILPETI LIVTLLVVLL ADLIQGRQAD RWTPYFAIVG LGGAIATMIP
LWTQPATISF FGSFISDHLS LFFRGLIALS ALGTILMSIR YVEQTGSSLG EFMTILLTAT
VGGMFIAGAQ ELVFIFVALE TLSIASYLLT GYTKRDSRSN EAALKYLLIG AASSAIFLYG
SSLLYGLSGG HTQLPAIAQA LSSESLGLVV ALVFVIAGIS FKISAVPFHQ WTPDVYEGAP
TPVVAFLSVG SKAAGFALAI RFLTLAFPSV TDQWQLIFTV LAILSMILGN VVALAQTSMK
RMLAYSSIGQ AGFVMIGFVV GTEAGYASML FYLLVYLFMN LGAFTCVILF SLRTGTDQIS
EYAGLYQKDP LLTLGLSLCL LSLGGIPPLA GFFGKIYLFW AGWQAGAYGL VLLGLLTSVI
SIYYYIRVVK MMVVKEPQEM SEAVRNYPEV SWSSFGLRPL QVGLVMTVIA TSLAGILANP
LFNLVNTAVW DVPQLANQPT VMEVAYQALS PAGKS
