NUOH2_KORVE
ID NUOH2_KORVE Reviewed; 354 AA.
AC Q1IS40;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=NADH-quinone oxidoreductase subunit H 2 {ECO:0000255|HAMAP-Rule:MF_01350};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01350};
DE AltName: Full=NADH dehydrogenase I subunit H 2 {ECO:0000255|HAMAP-Rule:MF_01350};
DE AltName: Full=NDH-1 subunit H 2 {ECO:0000255|HAMAP-Rule:MF_01350};
GN Name=nuoH2 {ECO:0000255|HAMAP-Rule:MF_01350};
GN OrderedLocusNames=Acid345_1308;
OS Koribacter versatilis (strain Ellin345).
OC Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC Candidatus Koribacter.
OX NCBI_TaxID=204669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin345;
RX PubMed=19201974; DOI=10.1128/aem.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is believed to be
CC ubiquinone. Couples the redox reaction to proton translocation (for
CC every two electrons transferred, four hydrogen ions are translocated
CC across the cytoplasmic membrane), and thus conserves the redox energy
CC in a proton gradient. This subunit may bind ubiquinone.
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01350};
CC -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H,
CC J, K, L, M, N constitute the membrane sector of the complex.
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01350}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01350}.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family.
CC {ECO:0000255|HAMAP-Rule:MF_01350}.
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DR EMBL; CP000360; ABF40310.1; -; Genomic_DNA.
DR RefSeq; WP_011522112.1; NC_008009.1.
DR AlphaFoldDB; Q1IS40; -.
DR SMR; Q1IS40; -.
DR STRING; 204669.Acid345_1308; -.
DR EnsemblBacteria; ABF40310; ABF40310; Acid345_1308.
DR KEGG; aba:Acid345_1308; -.
DR eggNOG; COG1005; Bacteria.
DR HOGENOM; CLU_015134_0_1_0; -.
DR OMA; WSGWASN; -.
DR OrthoDB; 1559067at2; -.
DR Proteomes; UP000002432; 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:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR HAMAP; MF_01350; NDH1_NuoH; 1.
DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR PANTHER; PTHR11432; PTHR11432; 1.
DR Pfam; PF00146; NADHdh; 1.
DR PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Ubiquinone.
FT CHAIN 1..354
FT /note="NADH-quinone oxidoreductase subunit H 2"
FT /id="PRO_5000121137"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01350"
SQ SEQUENCE 354 AA; 38997 MW; 7A6E0C66217C0F28 CRC64;
MGSIALFLLV ALIKVVLVIF VLLTAVAYTV WLERKVVGRM QNRWGPTRVG PFGLLQPLAD
GLKFILKEDL LPPHVNKPLY ILAPMLAVAM ALLSISIVPF GGTLTIGHIT TPLQITGIMG
ANGQPVDINI GLLIILGVTS IGVYGIALAG WSSNSKYSLL GSLRASAQMV SYEVSLGLSL
VGVLLLSGSF SLREIVRLQQ GGFWNWNIFG GFQFIAFFIY LTSAYAETNR IPFDLPEAET
ELVAGYHTEY SSMKFAMFFM AEYANMVTVA CIASILFLGG WSGPVPGFLP PILQSLVPVF
WFCLRIFAFL FIYIWVRGTL PRFRYDQLMA FSWKFLLPLS IANIMVTALF VALK
