NADH-quinone oxidoreductase subunit G - Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)

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
Ordered Locus Names:	bbp_148

Organism

Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]

Taxonomic identifier

224915 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	907 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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.
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 By similarity.
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
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome
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 – 907

907

NADH-quinone oxidoreductase subunit G

PRO_0000118544

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

Q89AU1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 021643AD31F32E43
Show »

FASTA

907

103,415

        10         20         30         40         50         60 
MTIIFVDNEE YNVDKSDNLL QACLSSGINI PYFCWHPVLG SIGSCRQCAV TIYKDLEDKV 

        70         80         90        100        110        120 
GQLVMSCMTS VLDGMIVSTS DKISRNFRKG IIELLMLNHP HDCPICEEGG SCHLQDMTVM 

       130        140        150        160        170        180 
AGHTVRRYRF TKRTHKNQYL GHFITHEMNR CISCYRCVRY YKDYSGGTDL GVFGISNNVY 

       190        200        210        220        230        240 
FGRYNDGCLE SEFSGNLVEV CPTGVFTDKT YSKKYSRKWD MQYAPSICQH CCVGCNISVG 

       250        260        270        280        290        300 
EKYGKISRIE NRYHNAINHY FLCDLGRFSY DYSNVDERLT YSIYRSQNKT KIINDVNKTI 

       310        320        330        340        350        360 
DKLAMKFKKS SKIIGIGSCR ASVESNFSLQ KLVGSENFYL GISQKEYDCL MLIKDILKDN 

       370        380        390        400        410        420 
QIHVPTLREI EKSDVIFLLG EDVTKTSPLI ALSIRQSIKG QVKTQDVSKN IPIWHADAVK 

       430        440        450        460        470        480 
NSFRNNKNKL FITNLMNSSL DDIADESYYA STFDQVLLGA EVYKCISNNC ISNVTLLKQD 

       490        500        510        520        530        540 
LLSCAKRIAT ALTLSKCPLI ISGSHSYNLD LIKVSFNIAK SLKVIGKNVG LILLSSNVNS 

       550        560        570        580        590        600 
IGVSLLEGIS IEKVINKVLL KQIDKIIVLE NDLYRYLPES IVDTLFKSSS CTVVIDHLNT 

       610        620        630        640        650        660 
RTLKQADIAI PTCNSFESSG TVVNYEGRAQ RFFKTYHPNS SENKKSILES WKWLHLLYCK 

       670        680        690        700        710        720 
LHKISVFWHS LDDVIEEISL KIFSFSKLKD VAPNSSFKIF GQKLARSHHR ASGRTALYSN 

       730        740        750        760        770        780 
INIHEPRPPQ DNDTMFSFSM EGCQNVQNYL PYVPFSWFPG WNSVQSWNTY KKINNENYGK 

       790        800        810        820        830        840 
HLFQDTTKFV LTYYKLNCKN VNKIEDLYLI VPCYFLFCNN ELAQYSPVIQ ENVLKNAYGI 

       850        860        870        880        890        900 
INTEDAKVLL IESGSKIEFS YLNKNFSIKV QLSKEFKKGQ LGLPLGMADF PFFLAEKQVK 


VFRKISI

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References

[1]

"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed: 12522265] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016826 Genomic DNA. Translation: AAO26882.1.
RefSeq	NP_777777.1. NC_004545.1.
3D structure databases
ProteinModelPortal	Q89AU1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000002249; EBBUCP00000002073; EBBUCG00000002249.
GeneID	1058511.
GenomeReviews	Gene locus bbp_148 in contig AE016826_GR.
KEGG	bab:bbp148.
PATRIC	21245075. VBIBucAph80364_0144.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000008121.
HOGENOM	HBG488172.
OMA	PSICHGC.
PhylomeDB	Q89AU1.
ProtClustDB	PRK08166.
Enzyme and pathway databases
BioCyc	BAPH224915:BBP_148-MONOMER.
Family and domain databases
InterPro	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:3.10.20.30. Ferredoxin_fold. 1 hit.
KO	K00336.
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	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_BUCBP

Accession

Primary (citable) accession number: Q89AU1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 65 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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents