NDHH2_GLOVI
ID NDHH2_GLOVI Reviewed; 394 AA.
AC Q7NI01;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit H 2 {ECO:0000255|HAMAP-Rule:MF_01358};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01358};
DE AltName: Full=NAD(P)H dehydrogenase subunit H 2;
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit H 2 {ECO:0000255|HAMAP-Rule:MF_01358};
DE AltName: Full=NDH-1 subunit H 2 {ECO:0000255|HAMAP-Rule:MF_01358};
DE Short=NDH-H 2 {ECO:0000255|HAMAP-Rule:MF_01358};
GN Name=ndhH2 {ECO:0000255|HAMAP-Rule:MF_01358}; OrderedLocusNames=gll2383;
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_01358}.
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_01358};
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_01358};
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_01358}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01358}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01358}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01358}.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01358}.
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DR EMBL; BA000045; BAC90324.1; -; Genomic_DNA.
DR RefSeq; NP_925329.1; NC_005125.1.
DR RefSeq; WP_011142379.1; NC_005125.1.
DR AlphaFoldDB; Q7NI01; -.
DR SMR; Q7NI01; -.
DR STRING; 251221.35212951; -.
DR EnsemblBacteria; BAC90324; BAC90324; BAC90324.
DR KEGG; gvi:gll2383; -.
DR PATRIC; fig|251221.4.peg.2422; -.
DR eggNOG; COG0649; Bacteria.
DR HOGENOM; CLU_015134_1_2_3; -.
DR InParanoid; Q7NI01; -.
DR OMA; GGRMHYM; -.
DR OrthoDB; 473681at2; -.
DR PhylomeDB; Q7NI01; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.645.10; -; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR PANTHER; PTHR11993; PTHR11993; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR TIGRFAMs; TIGR01962; NuoD; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; NADP; Plastoquinone;
KW Quinone; Reference proteome; Translocase; Transport.
FT CHAIN 1..394
FT /note="NAD(P)H-quinone oxidoreductase subunit H 2"
FT /id="PRO_0000371873"
SQ SEQUENCE 394 AA; 44893 MW; 738CC774953C2135 CRC64;
MVTIETRADQ MVLNLGPHHP STHGVLRLIV TLDGENVVDC RPVLGYLHRG MEKIGENRTI
IQYLPYCSRW DYAAAMMNEA PVVNAPEAMA GVKVPRRASY IRVIMLELSR IANHLLWVGP
FLLDMGAQSP FFYILREREL ILDLFEAATG LRMVGNNYFR VGGVTVDLPY GWVDKAHDLC
DVIPGKIDEY ERLITNNPIF RRRIENLGYI SREDAINWGL SGPMLRASGV KWDLRKVDHY
EIYDELDWDI AWDTGGDCLA RYIVRIKEMR ESVKIIRQAL DQLPGGPYEQ LEARRLAEGP
KSEWNSFDYQ FIGKKSSPTF KIPTGEYYAR SEEAKGELGI YVVGRDDTTP WRWKIRTPDF
ANLAILPMIL QGTKVADLVV VLGSIDIIMG SVDR
