NDHH1_GLOVI
ID NDHH1_GLOVI Reviewed; 393 AA.
AC Q7NI12;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit H 1 {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 1;
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit H 1 {ECO:0000255|HAMAP-Rule:MF_01358};
DE AltName: Full=NDH-1 subunit H 1 {ECO:0000255|HAMAP-Rule:MF_01358};
DE Short=NDH-H 1 {ECO:0000255|HAMAP-Rule:MF_01358};
GN Name=ndhH1 {ECO:0000255|HAMAP-Rule:MF_01358}; OrderedLocusNames=glr2372;
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; BAC90313.1; -; Genomic_DNA.
DR RefSeq; NP_925318.1; NC_005125.1.
DR RefSeq; WP_011142368.1; NC_005125.1.
DR AlphaFoldDB; Q7NI12; -.
DR SMR; Q7NI12; -.
DR STRING; 251221.35212940; -.
DR PRIDE; Q7NI12; -.
DR EnsemblBacteria; BAC90313; BAC90313; BAC90313.
DR KEGG; gvi:glr2372; -.
DR PATRIC; fig|251221.4.peg.2411; -.
DR eggNOG; COG0649; Bacteria.
DR HOGENOM; CLU_015134_1_2_3; -.
DR InParanoid; Q7NI12; -.
DR OMA; IMGTSME; -.
DR OrthoDB; 473681at2; -.
DR PhylomeDB; Q7NI12; -.
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; 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.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; NADP; Plastoquinone;
KW Quinone; Reference proteome; Translocase; Transport.
FT CHAIN 1..393
FT /note="NAD(P)H-quinone oxidoreductase subunit H 1"
FT /id="PRO_0000357826"
SQ SEQUENCE 393 AA; 45016 MW; 5DC88A3F1BF57612 CRC64;
MSMLETRAER MVINLGPHHP SMHGVLRLIV TLDGENVVDC VPVLGYLHRS MEKIAESRTI
IQYLPYVTRW DYLATMFTEA ITVNAPEQLA GVQVPRRARY IRVIMLELSR IASHLLWLGP
FMADIGATSP FFYIFREREM IYDLFEAATG MRMMHNYFRV GGVAVDLPYG WVDKARDFCN
YLPPKIDEYE RLITNNPIFR GRVEGLGYIG REDAINWGLS GPMLRASGVN WDLRKVDHYE
IYDELDWNVA WDTGGDTLAR YVVRIQEMRE SVKMIRQALD QLPGGPYENL EAQRLSGGPK
SEWNGFDYQF IGKKSSPTFK MPRGEHYVRV EAPKGELGVY LIGDDSTFPW RWKIRPPGFI
NLAVLPKLVQ GTKLADLMAI LGSVDIIMGE VDR
