ID   NU2C_GLOVI              Reviewed;         513 AA.
AC   Q7NGP8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=glr3120;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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: Cell inner 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; BA000045; BAC91061.1; -; Genomic_DNA.
DR   RefSeq; NP_926066.1; NC_005125.1.
DR   RefSeq; WP_011143113.1; NC_005125.1.
DR   AlphaFoldDB; Q7NGP8; -.
DR   SMR; Q7NGP8; -.
DR   STRING; 251221.35213691; -.
DR   EnsemblBacteria; BAC91061; BAC91061; BAC91061.
DR   KEGG; gvi:glr3120; -.
DR   PATRIC; fig|251221.4.peg.3150; -.
DR   eggNOG; COG1007; Bacteria.
DR   HOGENOM; CLU_007100_1_2_3; -.
DR   InParanoid; Q7NGP8; -.
DR   OMA; FYIRVIV; -.
DR   OrthoDB; 1664448at2; -.
DR   PhylomeDB; Q7NGP8; -.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma 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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; NADP; Plastoquinone;
KW   Quinone; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..513
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 2"
FT                   /id="PRO_0000225353"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        300..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        456..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   REGION          494..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  54857 MW;  1D3BD2A5D19054E5 CRC64;
     MNIDLAALNA GTLWPEYIVT ITLIVVLLVD LISGRKASWS LPYLALLGLG IATATLLPMW
     ILENPVSFLG SFTADPLSVV FRAFILISAA LTVLMSVRYI NQSSLATAEF YVLLLGATLG
     AMLLSGSSEM AMIFVALELL SITSYLLSGY AKLDKRSNEA SLKYLLIGAA SSGIFLYGMS
     LLYGFSGGQT QLTEIAPRIV NLGFPALLSL VLVAAGICFK LSAVPFHQWT PDVYEGSPTP
     VVAFLSVGSK AAGFALAIRF MTSAYPGFSE QWQTLFVLLA ILSMVLGNVV AIAQTSMKRM
     LAYSSIAQAG YVMIGLAIGT QEGYSSMILY IGTYLFMNLG AFMAVVLFSL RTGTDEITAY
     SGLYQKDPFL TLVLSLCLLS LAGIPPLAGF FGKLYLFWAA VQSQAYTLVF FGLVTSVASI
     YYYVRVVKLM LVKEPSPQVL AYSEAGDQDG IQTLKAGMLI TTVATVVLGI LFPPLISLAD
     TSLRATPSLQ QVRTATPVSR VSTGAQAPAD HGR