NADH-quinone oxidoreductase subunit G - Pseudomonas fluorescens

Preferred order of sections

Names and origin

Protein names

Recommended name:
NADH-quinone oxidoreductase subunit G
EC=1.6.99.5

Alternative name(s):
NADH dehydrogenase I subunit G
NDH-1 subunit G

Gene names

Name:

nuoG

Organism

Pseudomonas fluorescens

Taxonomic identifier

294 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	904 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 By similarity. Required for plants roots colonization. Ref.1
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.
Induction	By low oxygen growth conditions, especially in rhizosphere. Ref.1
Sequence similarities	Belongs to the complex I 75 kDa subunit family. Contains 1 2Fe-2S ferredoxin-type domain.

Ontologies

Keywords
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Gene Ontology (GO)
Biological process	ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro
Cellular component	membrane Inferred from electronic annotation. Source: InterPro
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinone binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 904

904

NADH-quinone oxidoreductase subunit G

PRO_0000118550

Regions

Domain

1 – 83

83

2Fe-2S ferredoxin-type

Sites

Metal binding

34

1

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

45

1

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

48

1

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

67

1

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

99

1

Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity

Metal binding

103

1

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

106

1

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

112

1

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

151

1

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

154

1

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

157

1

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

201

1

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

228

1

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

231

1

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

235

1

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

263

1

Iron-sulfur 4 (4Fe-4S) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q9KGW3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C25E86C6D4DFA457
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FASTA

904

98,158

        10         20         30         40         50         60 
MATIHVDGKE LEVDGADNLL QACLSLGLDI PYFCWHPALG SVGACRQCAV KQYTDENDKR 

        70         80         90        100        110        120 
GRIVMSCMTP ATDGSWISID DEEAKVFRAS VVEWLMTNHP HDCPVCEEGG HCHLQDMTVM 

       130        140        150        160        170        180 
TGHNERRYRF TKRTHQNQDL GPFISHEMNR CIACYRCVRF YKDYAGGTDL GVFGAHDNVY 

       190        200        210        220        230        240 
FGRVEDGTLE SEFSGNLTEV CPTGVFTDKT HSERYNRKWD MQFSPSICHG CSSGCNISPG 

       250        260        270        280        290        300 
ERYGELRRIE NRFNGSVNQY FLCDRGRFGY GYVNRKDRPR QPLLANGAKL SLDQALDKAA 

       310        320        330        340        350        360 
ELLRGRNIVG IGSPRASLES NYALRELVGA EHFYSGIEAG ELERIRLVLQ VLKDSPLPVP 

       370        380        390        400        410        420 
NMRDIEDHDA VFVLGEDLTQ TAARMALALR QSVKGKAEDM ADAMRVQPWL DAAVKNIGQH 

       430        440        450        460        470        480 
ALNPLFIASL AETKLDDVAE ECVHAAPDDL ARIGFAVAHA LDASAPAVDG LDSEAAALAQ 

       490        500        510        520        530        540 
RIADALLAAK RPLIIAGTSL GSKALIEAAA NIAKALKLRE KNGSISLIVP EANSLGLAML 

       550        560        570        580        590        600 
GGESVDAALQ AVIDGSADAI VVLENDLYTR TDKAKVDAAL NAAKVLIVAD HQKTATTDRA 

       610        620        630        640        650        660 
HLVLPAASFA EGDGTLVSQE GRAQRFFQVF DPQYLDASIL VHEGWRWLHA LRATLLDQPI 

       670        680        690        700        710        720 
DWTQLDHVTA AVASSSPQLA AIVDAAPSAS FRIKGLKLAR EPLRYSGRTA MRADISVHEP 

       730        740        750        760        770        780 
RTSQDNDTAF SFSMEGYSGS TEPRSQVPFA WSPGWNSPQA WNKFQDEVGG HLRAGDPGTR 

       790        800        810        820        830        840 
LIESQGDHLS WFASVPRAFN PAPGTWQVVP FHHLFGSEEN SSKAAPVQER IPAAYVSLAK 

       850        860        870        880        890        900 
SEADRLGVND GALLSLNVAG QTLRLPLRIN EELGAGLVAL PAGLAGIPPA IFGKTVDGLQ 


EAAQ

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References

[1]

"Characterization of NADH dehydrogenases of Pseudomonas fluorescens WCS365 and their role in competitive root colonization."
Camacho-Carvajal M.M., Wijfjes A.H.M., Mulders I.H.M., Lugtenberg B.J.J., Bloemberg G.V.
Mol. Plant Microbe Interact. 15:662-671(2002) [PubMed: 12118882] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
Strain: WCS365.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF281148 Genomic DNA. Translation: AAF97803.1.
3D structure databases
ProteinModelPortal	Q9KGW3.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR009010. Asp_de-COase-like_fold. IPR012675. Beta-grasp_ferredoxin-type. IPR001041. Ferredoxin. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4_dom. IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS. IPR010228. NADH_UbQ_OxRdtase_Gsu. IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. [Graphical view]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF00111. Fer2. 1 hit. PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
SMART	SM00926. Molybdop_Fe4S4. 1 hit. SM00929. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit. SSF54292. Ferredoxin. 1 hit.
TIGRFAMs	TIGR01973. NuoG. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. 1 hit. PS00641. COMPLEX1_75K_1. 1 hit. PS00642. COMPLEX1_75K_2. 1 hit. PS00643. COMPLEX1_75K_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUOG_PSEFL

Accession

Primary (citable) accession number: Q9KGW3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	October 1, 2000
Last modified:	November 16, 2011
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents