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P33602 (NUOG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NADH-quinone oxidoreductase subunit G

EC=1.6.99.5
Alternative name(s):
NADH dehydrogenase I subunit G
NDH-1 subunit G
NUO7
Gene names
Name:nuoG
Ordered Locus Names:b2283, JW2278
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length908 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.

Catalytic activity

NADH + quinone = NAD+ + quinol.

Cofactor

Binds 1 2Fe-2S cluster per subunit By similarity.

Binds 3 4Fe-4S clusters per subunit By similarity.

Subunit structure

Composed of 13 different subunits. Subunits NuoCD, E, F, and G constitute the peripheral sector of the complex.

Subcellular location

Cytoplasm. Cell inner membrane; Peripheral membrane protein Ref.7.

Sequence similarities

Belongs to the complex I 75 kDa subunit family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 4Fe-4S Mo/W bis-MGD-type domain.

Sequence caution

The sequence BAA16111.2 differs from that shown. Reason: Erroneous initiation.

The sequence CAA48366.1 differs from that shown. Reason: Frameshift at positions 715 and 806.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 908907NADH-quinone oxidoreductase subunit G
PRO_0000118546

Regions

Domain2 – 83822Fe-2S ferredoxin-type
Domain221 – 277574Fe-4S Mo/W bis-MGD-type

Sites

Metal binding341Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding451Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding481Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding671Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding991Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
Metal binding1031Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1061Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1121Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1511Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1541Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1571Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2011Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2281Iron-sulfur 4 (4Fe-4S) By similarity
Metal binding2311Iron-sulfur 4 (4Fe-4S) By similarity
Metal binding2351Iron-sulfur 4 (4Fe-4S) By similarity
Metal binding2631Iron-sulfur 4 (4Fe-4S) By similarity

Experimental info

Sequence conflict1881T → Q in CAA48366. Ref.1
Sequence conflict2101T → K in CAA48366. Ref.1
Sequence conflict3901Missing in CAA48366. Ref.1
Sequence conflict6481S → T in CAA48366. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P33602 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 7B8626E19709D540

FASTA908100,299
        10         20         30         40         50         60 
MATIHVDGKE YEVNGADNLL EACLSLGLDI PYFCWHPALG SVGACRQCAV KQYQNAEDTR 

        70         80         90        100        110        120 
GRLVMSCMTP ASDGTFISID DEEAKQFRES VVEWLMTNHP HDCPVCEEGG NCHLQDMTVM 

       130        140        150        160        170        180 
TGHSFRRYRF TKRTHRNQDL GPFISHEMNR CIACYRCVRY YKDYADGTDL GVYGAHDNVY 

       190        200        210        220        230        240 
FGRPEDGTLE SEFSGNLVEI CPTGVFTDKT HSERYNRKWD MQFAPSICQQ CSIGCNISPG 

       250        260        270        280        290        300 
ERYGELRRIE NRYNGTVNHY FLCDRGRFGY GYVNLKDRPR QPVQRRGDDF ITLNAEQAMQ 

       310        320        330        340        350        360 
GAADILRQSK KVIGIGSPRA SVESNFALRE LVGEENFYTG IAHGEQERLQ LALKVLREGG 

       370        380        390        400        410        420 
IYTPALREIE SYDAVLVLGE DVTQTGARVA LAVRQAVKGK AREMAAAQKV ADWQIAAILN 

       430        440        450        460        470        480 
IGQRAKHPLF VTNVDDTRLD DIAAWTYRAP VEDQARLGFA IAHALDNSAP AVDGIEPELQ 

       490        500        510        520        530        540 
SKIDVIVQAL AGAKKPLIIS GTNAGSLEVI QAAANVAKAL KGRGADVGIT MIARSVNSMG 

       550        560        570        580        590        600 
LGIMGGGSLE EALTELETGR ADAVVVLEND LHRHASAIRV NAALAKAPLV MVVDHQRTAI 

       610        620        630        640        650        660 
MENAHLVLSA ASFAESDGTV INNEGRAQRF FQVYDPAYYD SKTVMLESWR WLHSLHSTLL 

       670        680        690        700        710        720 
SREVDWTQLD HVIDAVVAKI PELAGIKDAA PDATFRIRGQ KLAREPHRYS GRTAMRANIS 

       730        740        750        760        770        780 
VHEPRQPQDI DTMFTFSMEG NNQPTAHRSQ VPFAWAPGWN SPQAWNKFQD EVGGKLRFGD 

       790        800        810        820        830        840 
PGVRLFETSE NGLDYFTSVP ARFQPQDGKW RIAPYYHLFG SDELSQRAPV FQSRMPQPYI 

       850        860        870        880        890        900 
KLNPADAAKL GVNAGTRVSF SYDGNTVTLP VEIAEGLTAG QVGLPMGMSG IAPVLAGAHL 


EDLKEAQQ 

« Hide

References

« Hide 'large scale' references
[1]"The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I."
Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.
J. Mol. Biol. 233:109-122(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / AN387.
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect growth on mixed amino acids."
Pruss B.M., Nelms J.M., Park C., Wolfe A.J.
J. Bacteriol. 176:2143-2150(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-170.
[6]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Strain: K12 / EMG2.
[7]"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: BL21-DE3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68301 Genomic DNA. Translation: CAA48366.1. Frameshift.
U00096 Genomic DNA. Translation: AAC75343.2.
AP009048 Genomic DNA. Translation: BAA16111.2. Different initiation.
L25055 Unassigned DNA. Translation: AAA03538.1.
PIRA65000.
RefSeqNP_416786.4. NC_000913.3.
YP_490523.1. NC_007779.1.

3D structure databases

ProteinModelPortalP33602.
SMRP33602. Positions 1-234.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid851103. 1 interaction.
DIPDIP-10383N.
IntActP33602. 31 interactions.
MINTMINT-1244767.
STRING511145.b2283.

Protein family/group databases

TCDB3.D.1.1.1. the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.

Proteomic databases

PaxDbP33602.
PRIDEP33602.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75343; AAC75343; b2283.
BAA16111; BAA16111; BAA16111.
GeneID12931518.
946762.
KEGGecj:Y75_p2247.
eco:b2283.
PATRIC32119933. VBIEscCol129921_2376.

Organism-specific databases

EchoBASEEB2011.
EcoGeneEG12087. nuoG.

Phylogenomic databases

eggNOGCOG1034.
HOGENOMHOG000276177.
KOK00336.
OMAGYGYVNR.
OrthoDBEOG6CVV7G.
PhylomeDBP33602.
ProtClustDBPRK08166.

Enzyme and pathway databases

BioCycEcoCyc:NUOG-MONOMER.
ECOL316407:JW2278-MONOMER.
MetaCyc:NUOG-MONOMER.

Gene expression databases

GenevestigatorP33602.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR009010. Asp_de-COase-like_dom.
IPR012675. Beta-grasp_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
IPR010228. NADH_UbQ_OxRdtase_Gsu.
IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
[Graphical view]
PfamPF04879. Molybdop_Fe4S4. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTSM00926. Molybdop_Fe4S4. 1 hit.
SM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMSSF50692. SSF50692. 1 hit.
SSF54292. SSF54292. 1 hit.
TIGRFAMsTIGR01973. NuoG. 1 hit.
PROSITEPS51085. 2FE2S_FER_2. 1 hit.
PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00641. COMPLEX1_75K_1. 1 hit.
PS00642. COMPLEX1_75K_2. 1 hit.
PS00643. COMPLEX1_75K_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP33602.

Entry information

Entry nameNUOG_ECOLI
AccessionPrimary (citable) accession number: P33602
Secondary accession number(s): P76489, P78184, P78185
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 141 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene