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Links from Protein

Items: 19

1.

NADH-quinone oxidoreductase subunit 3, ferredoxin-like domain

NADH-quinone oxidoreductase subunit 3 (Nqo3) is a component of respiratory complex I. This protein is located at the peripheral arm of the complex and consists of multiple domains. This entry represents the second ferredoxin-like domain which contains Fe4-S4 cluster, one of the redox centers of the complex [1-5]. Paper describing PDB structure 2fug. [1]. 16469879. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Sazanov LA, Hinchliffe P;. Science. 2006;311:1430-1436. Paper describing PDB structure 5lc5. [2]. 27509854. Structure of mammalian respiratory complex I. Zhu J, Vinothkumar KR, Hirst J;. Nature. 2016;536:354-358. Paper describing PDB structure 5lnk. [3]. 27595392. Atomic structure of the entire mammalian mitochondrial complex I. Fiedorczuk K, Letts JA, Degliesposti G, Kaszuba K, Skehel M, Sazanov LA;. Nature. 2016;538:406-410. Paper describing PDB structure 5o31. [4]. 29395787. Structure of the Deactive State of Mammalian Respiratory Complex I. Blaza JN, Vinothkumar KR, Hirst J;. Structure. 2018;26:312-319. Paper describing PDB structure 5xtb. [5]. 28844695. Architecture of Human Mitochondrial Respiratory Megacomplex I2III2IV2. Guo R, Zong S, Wu M, Gu J, Yang M;. Cell. 2017;170:1247-1257. (from Pfam)

Date:
2024-10-16
Family Accession:
NF047104.1
Method:
HMM
2.

NADH-ubiquinone oxidoreductase NDSU1/NuoG-like, 4Fe-4S domain

This entry represents the 4Fe-4S domain of NADH-ubiquinone oxidoreductase NDUFS1 from mammals and NuoG from bacteria, which are part of respiratory chain complex I [1-5]. Paper describing PDB structure 2fug. [1]. 16469879. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Sazanov LA, Hinchliffe P;. Science. 2006;311:1430-1436. Paper describing PDB structure 4ydd. [2]. 26940877. Perchlorate Reductase Is Distinguished by Active Site Aromatic Gate Residues. Youngblut MD, Tsai CL, Clark IC, Carlson HK, Maglaqui AP, Gau-Pan PS, Redford SA, Wong A, Tainer JA, Coates JD;. J Biol Chem. 2016;291:9190-9202. Paper describing PDB structure 5lnk. [3]. 27595392. Atomic structure of the entire mammalian mitochondrial complex I. Fiedorczuk K, Letts JA, Degliesposti G, Kaszuba K, Skehel M, Sazanov LA;. Nature. 2016;538:406-410. Paper describing PDB structure 5o31. [4]. 29395787. Structure of the Deactive State of Mammalian Respiratory Complex I. Blaza JN, Vinothkumar KR, Hirst J;. Structure. 2018;26:312-319. Paper describing PDB structure 5t5i. [5]. 27846502. The methanogenic CO2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters. Wagner T, Ermler U, Shima S;. Science. 2016;354:114-117. (from Pfam)

Date:
2024-10-16
Family Accession:
NF046677.1
Method:
HMM
3.

2Fe-2S iron-sulfur cluster-binding protein

The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins. (from Pfam)

Date:
2024-08-14
Family Accession:
NF024900.5
Method:
HMM
4.

NADH-ubiquinone oxidoreductase-G iron-sulfur binding region

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2024-08-14
Family Accession:
NF022058.5
Method:
HMM
5.

NADH-ubiquinone oxidoreductase subunit G, C-terminal

Members of this family of are found at the C-terminus of NADH dehydrogenases subunit G or NADH-ubiquinone oxidoreductase subunit G. EC:1.6.99.5. (from Pfam)

GO Terms:
Molecular Function:
oxidoreductase activity, acting on NAD(P)H (GO:0016651)
Molecular Function:
iron-sulfur cluster binding (GO:0051536)
Date:
2024-08-14
Family Accession:
NF020884.5
Method:
HMM
6.

2Fe-2S iron-sulfur cluster-binding protein

GO Terms:
Molecular Function:
iron-sulfur cluster binding (GO:0051536)
Date:
2024-08-14
Family Accession:
NF012339.5
Method:
HMM
7.

molybdopterin-dependent oxidoreductase

GO Terms:
Molecular Function:
oxidoreductase activity (GO:0016491)
Date:
2024-08-14
Family Accession:
NF012602.5
Method:
HMM
8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.
new record, indexing in progress
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12.
new record, indexing in progress
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13.
new record, indexing in progress
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14.
new record, indexing in progress
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15.
new record, indexing in progress
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16.
new record, indexing in progress
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17.
new record, indexing in progress
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18.

NADH-quinone oxidoreductase subunit NuoG

This HMM represents the G subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria while translocating protons, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This HMM excludes related subunits from formate dehydrogenase complexes.

Gene:
nuoG
GO Terms:
Biological Process:
mitochondrial electron transport, NADH to ubiquinone (GO:0006120)
Molecular Function:
NADH:ubiquinone reductase (non-electrogenic) activity (GO:0050136)
Molecular Function:
iron-sulfur cluster binding (GO:0051536)
Date:
2024-06-14
Family Accession:
TIGR01973.1
Method:
HMM
19.

NuoG family protein

NuoG family protein

Date:
2017-03-02
Family Accession:
11437111
Method:
Sparcle
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