nuoG:Gene Product(s)
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Nomenclature | Function | Interactions | Localization | Sequence | Domains | Structure | Resources | Accessions | Links | References | Suggestions |
Nomenclature
See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.
Standard name |
NuoG |
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Synonyms |
NADH:ubiquinone oxidoreductase, chain G[1], B2283[2][1], NuoG[2][1] , ECK2277, JW2278, b2283 |
Product description |
Component of soluble NADH dehydrogenase fragment[3]; NADH dehydrogenase I[2][3] NADH:ubiquinone oxidoreductase subunit G, complex I; NADH dehydrogenase I[4] |
EC number (for enzymes) |
1.6.5.3[1] |
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Notes
Function
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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.
Qualifier | GO ID | GO term name | Reference | Evidence Code | with/from | Aspect | Notes | Status |
---|---|---|---|---|---|---|---|---|
NOT |
GO:0005737 |
cytoplasm |
IDA: Inferred from Direct Assay |
C |
Seeded from Riley et al 2006 [1]. See discussion page for explanation of 'NOT' qualifier. |
complete | ||
GO:0030964 |
NADH dehydrogenase complex |
IDA: Inferred from Direct Assay |
C |
The E. coli NADH dehydrogenase complex was purified and the subunits separated by SDS-PAGE. The N-termini of these 6 polypeptides were sequenced after deblocking with methanolic HCl. |
complete | |||
GO:0005886 |
plasma membrane |
IDA: Inferred from Direct Assay |
C |
The NADH dehydrogenase I complex fractionates with cytoplasmic membranes. |
complete | |||
GO:0005506 |
iron ion binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
Contributes to |
GO:0003954 |
NADH dehydrogenase activity |
IDA: Inferred from Direct Assay |
F |
Purified NADH dehydrogenase I in membrane vesicles can oxidize NADH. |
complete | ||
GO:0005737 |
cytoplasm |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0051539 |
4 iron, 4 sulfur cluster binding |
IDA: Inferred from Direct Assay |
F |
EPR spectra from purified NuoG reduced by dithionite gave evidence of two rhombic [4Fe-4S] clusters (Fig. 2 and text). |
complete | |||
GO:0005737 |
cytoplasm |
IEA: Inferred from Electronic Annotation |
SP_SL:SL-0086 |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0051537 |
2 iron, 2 sulfur cluster binding |
IDA: Inferred from Direct Assay |
F |
EPR spectra from purified NuoG reduced by dithionite gave evidence of an axial [2Fe-2S] cluster (Fig. 2 and text). |
complete | |||
GO:0008137 |
NADH dehydrogenase (ubiquinone) activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
Contributes to |
GO:0010181 |
FMN binding |
IDA: Inferred from Direct Assay |
F |
The water-soluble NADH fragment contains the subunits NuoE, NuoF, and NuoG. This fragment also contains FMN and has the EPR-detectable FeS clusters N1b, N1c, N3, and N4. |
complete | ||
GO:0009055 |
electron carrier activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0016491 |
oxidoreductase activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0016491 |
oxidoreductase activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0016491 |
oxidoreductase activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0016491 |
oxidoreductase activity |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0016651 |
oxidoreductase activity, acting on NADH or NADPH |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0019898 |
extrinsic to membrane |
IEA: Inferred from Electronic Annotation |
SP_SL:SL-9903 |
C |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0030151 |
molybdenum ion binding |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0042773 |
ATP synthesis coupled electron transport |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0046872 |
metal ion binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0048038 |
quinone binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0050136 |
NADH dehydrogenase (quinone) activity |
GOA:spec |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0051537 |
2 iron, 2 sulfur cluster binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0051539 |
4 iron, 4 sulfur cluster binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0055114 |
oxidation reduction |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0055114 |
oxidation reduction |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0055114 |
oxidation reduction |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.
Partner Type | Partner | Notes | References | Evidence |
---|---|---|---|---|
Protein |
Subunits of soluble NADH dehydrogenase fragment |
could be indirect |
||
Protein |
skp |
LCMS(ID Probability):99.6 | ||
Protein |
leuD |
LCMS(ID Probability):99.6 | ||
Protein |
nadC |
LCMS(ID Probability):99.3 | ||
Protein |
purA |
LCMS(ID Probability):99.6 | ||
Protein |
purL |
LCMS(ID Probability):99.6 | ||
Protein |
nuoF |
LCMS(ID Probability):99.6 | ||
Protein |
nuoE |
LCMS(ID Probability):99.6 | ||
Protein |
Subunits of NADH dehydrogenase I |
could be indirect |
| |
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Notes
Localization
See Help:Product_localization for how to add or edit information in this section of EcoliWiki.
Compartment | Description | Evidence | Reference/Source | Notes |
---|---|---|---|---|
Cytoplasm |
| |||
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Notes
Structure and Physical Properties
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Physical Properties
See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.
Name | |
---|---|
Sequence |
MLMATIHVDG KEYEVNGADN LLEACLSLGL DIPYFCWHPA LGSVGACRQC AVKQYQNAED TRGRLVMSCM TPASDGTFIS IDDEEAKQFR ESVVEWLMTN HPHDCPVCEE GGNCHLQDMT VMTGHSFRRY RFTKRTHRNQ DLGPFISHEM NRCIACYRCV RYYKDYADGT DLGVYGAHDN VYFGRPEDGT LESEFSGNLV EICPTGVFTD KTHSERYNRK WDMQFAPSIC QQCSIGCNIS PGERYGELRR IENRYNGTVN HYFLCDRGRF GYGYVNLKDR PRQPVQRRGD DFITLNAEQA MQGAADILRQ SKKVIGIGSP RASVESNFAL RELVGEENFY TGIAHGEQER LQLALKVLRE GGIYTPALRE IESYDAVLVL GEDVTQTGAR VALAVRQAVK GKAREMAAAQ KVADWQIAAI LNIGQRAKHP LFVTNVDDTR LDDIAAWTYR APVEDQARLG FAIAHALDNS APAVDGIEPE LQSKIDVIVQ ALAGAKKPLI ISGTNAGSLE VIQAAANVAK ALKGRGADVG ITMIARSVNS MGLGIMGGGS LEEALTELET GRADAVVVLE NDLHRHASAI RVNAALAKAP LVMVVDHQRT AIMENAHLVL SAASFAESDG TVINNEGRAQ RFFQVYDPAY YDSKTVMLES WRWLHSLHST LLSREVDWTQ LDHVIDAVVA KIPELAGIKD AAPDATFRIR GQKLAREPHR YSGRTAMRAN ISVHEPRQPQ DIDTMFTFSM EGNNQPTAHR SQVPFAWAPG WNSPQAWNKF QDEVGGKLRF GDPGVRLFET SENGLDYFTS VPARFQPQDG KWRIAPYYHL FGSDELSQRA PVFQSRMPQP YIKLNPADAA KLGVNAGTRV SFSYDGNTVT LPVEIAEGLT AGQVGLPMGM SGIAPVLAGA HLEDLKEAQQ |
Length |
910 |
Mol. Wt |
100.543 kDa |
pI |
6.2 (calculated) |
Extinction coefficient |
109,210 - 111,210 (calc based on 29 Y, 12 W, and 16 C residues) |
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Domains/Motifs/Modification Sites
See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.
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Structure
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Structure figures<protect> | ||||||
Notes
Gene Product Resources
See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.
Resource type | Source | Notes/Reference |
---|---|---|
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Notes
Accessions in Other Databases
See Help:Gene_accessions for help with entering information into the Gene Accessions table.
Database | Accession | Notes |
---|---|---|
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
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Notes
Links
Name | URL | Comments |
---|---|---|
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References
See Help:References for how to manage references in EcoliWiki.
- ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 3.0 3.1 3.2 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ 5.0 5.1 5.2 5.3 Leif, H et al. (1995) Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli. Eur. J. Biochem. 230 538-48 PubMed
- ↑ Matsushita, K et al. (1987) NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry 26 7732-7 PubMed
- ↑ 7.0 7.1 Yakovlev, G et al. (2007) Reevaluating the relationship between EPR spectra and enzyme structure for the iron sulfur clusters in NADH:quinone oxidoreductase. Proc. Natl. Acad. Sci. U.S.A. 104 12720-5 PubMed
- ↑ 8.0 8.1 8.2 8.3 8.4 8.5 8.6 Hu, P et al. (2009) Global functional atlas of Escherichia coli encompassing previously uncharacterized proteins. PLoS Biol. 7 e96 PubMed
- ↑ Link, AJ et al. (1997) Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18 1259-313 PubMed
- ↑ Moreno-Bruna, B et al. (2001) Adenosine diphosphate sugar pyrophosphatase prevents glycogen biosynthesis in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 98 8128-32 PubMed
- ↑ 11.0 11.1 11.2 11.3 11.4 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed
Categories
- GO:0005737 ! cytoplasm
- GO:0030964 ! NADH dehydrogenase complex
- GO:0005886 ! plasma membrane
- GO:0005506 ! iron ion binding
- GO:0003954 ! NADH dehydrogenase activity
- GO:0051539 ! 4 iron, 4 sulfur cluster binding
- GO:0051537 ! 2 iron, 2 sulfur cluster binding
- GO:0008137 ! NADH dehydrogenase (ubiquinone) activity
- GO:0010181 ! FMN binding
- GO:0009055 ! electron transfer activity
- GO:0016491 ! oxidoreductase activity
- GO:0016651 ! oxidoreductase activity, acting on NAD(P)H
- GO:0019898 ! extrinsic component of membrane
- GO:0030151 ! molybdenum ion binding
- GO:0042773 ! ATP synthesis coupled electron transport
- GO:0046872 ! metal ion binding
- GO:0048038 ! quinone binding
- GO:0050136 ! NADH dehydrogenase (quinone) activity
- GO:0055114 ! oxidation-reduction process
- Proteins
- RefGenome Annotated Gene