(data stored in ACNUC7421 zone)

SWISSPROT: NUOH1_SYNFM

ID   NUOH1_SYNFM             Reviewed;         329 AA.
AC   A0LEQ2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JAN-2019, entry version 77.
DE   RecName: Full=NADH-quinone oxidoreductase subunit H 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01350};
DE   AltName: Full=NDH-1 subunit H 1 {ECO:0000255|HAMAP-Rule:MF_01350};
GN   Name=nuoH1 {ECO:0000255|HAMAP-Rule:MF_01350};
GN   OrderedLocusNames=Sfum_0203;
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC       sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC       immediate electron acceptor for the enzyme in this species is
CC       believed to be ubiquinone. Couples the redox reaction to proton
CC       translocation (for every two electrons transferred, four hydrogen
CC       ions are translocated across the cytoplasmic membrane), and thus
CC       conserves the redox energy in a proton gradient. This subunit may
CC       bind ubiquinone. {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,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01350};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits
CC       NuoA, H, J, K, L, M, N constitute the membrane sector of the
CC       complex. {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}.
DR   EMBL; CP000478; ABK15904.1; -; Genomic_DNA.
DR   RefSeq; WP_011697077.1; NC_008554.1.
DR   STRING; 335543.Sfum_0203; -.
DR   PRIDE; A0LEQ2; -.
DR   EnsemblBacteria; ABK15904; ABK15904; Sfum_0203.
DR   KEGG; sfu:Sfum_0203; -.
DR   eggNOG; ENOG4105CMZ; Bacteria.
DR   eggNOG; COG1005; LUCA.
DR   HOGENOM; HOG000228276; -.
DR   KO; K00337; -.
DR   OMA; AGWASAN; -.
DR   OrthoDB; 1559067at2; -.
DR   BioCyc; SFUM335543:G1G7I-206-MONOMER; -.
DR   Proteomes; UP000001784; 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; PS00667; COMPLEX1_ND1_1; 1.
DR   PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LEQ2.
DR   SWISS-2DPAGE; A0LEQ2.
KW   Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD;
KW   Quinone; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Ubiquinone.
FT   CHAIN         1    329       NADH-quinone oxidoreductase subunit H 1.
FT                                /FTId=PRO_0000299954.
FT   TRANSMEM     12     32       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM     81    101       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM    112    132       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM    152    172       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM    184    204       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM    244    264       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM    268    288       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
FT   TRANSMEM    303    323       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01350}.
SQ   SEQUENCE   329 AA;  36721 MW;  66843348B13F9BA1 CRC64;
     MGHEGGTEWV RLIVGLVIIL AFSQLNALFL VWLERKVAGR IQLRPGPMEV GPHGLLQTIM
     DGIKLVGKEL ITPRSVDRKL FILAPVLVFM PVLVGFLVLP FGPGLILRDM NVGILLIFSF
     STFTVLAILA GGWASNNKYA LLGAIRSVGQ NVAYEIPLLL TVMSVVLMVN SMRFSEIVAA
     QGRVWFIFLQ PVAGLLYLIC ATAETNRAPF DIPEAESELV AGFHTEYTGM RFGLFFLAEY
     TNMFIVTAVA TSLFFGGWHG PFGFDFGLPG VVWFLIKTYV LIFVIMWVRW TFPRIRFDQL
     MNFSWKFLIP VSLVNLVVTA VVLKLIDLN
//

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