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Q8K9Y2 (NUOG_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. 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·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
Gene names
Name:nuoG
Ordered Locus Names:BUsg_152
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length910 AA.
Sequence statusComplete.
Protein existenceInferred 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.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 910910NADH-quinone oxidoreductase subunit G
PRO_0000118543

Regions

Domain1 – 83832Fe-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) Potential
Metal binding2311Iron-sulfur 4 (4Fe-4S) Potential
Metal binding2351Iron-sulfur 4 (4Fe-4S) Potential
Metal binding2631Iron-sulfur 4 (4Fe-4S) Potential

Sequences

Sequence LengthMass (Da)Tools
Q8K9Y2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 7F50FE2F296DA519

FASTA910104,358
        10         20         30         40         50         60 
MAKIYVDGKA YCMSESDNLL QACLSSGLNI PYFCWHPILG SLGACRQCAV TQYNSSLDNQ 

        70         80         90        100        110        120 
GKLIMSCMTP VIDGTIISIN DDTSKKFRSN IVELLLTNHP HDCPVCEEGG NCHLQDMTVM 

       130        140        150        160        170        180 
TTHNFRNYRF SKRTHKNQYL GSFIKHEMNR CIGCYRCVRY YRDYADGTDL DVYGANNNIY 

       190        200        210        220        230        240 
FGRIEHGVLE NEHSGNLIEI CPTGVFTDKT HSKKYNRKWD MQYAPGICQN CSIGCNISIG 

       250        260        270        280        290        300 
ERYGEIRRIE NRYHESINHY LICDLGRFGY SHTNLKNRPK KPILSTKEND VNILNFNKAI 

       310        320        330        340        350        360 
EYATNFFQRY KNVIGVGSIR SSIENNFALQ ELVGKENFCN GMSDKENSCI KLILDTLKNN 

       370        380        390        400        410        420 
QLYIPSLKEI ESYDTILILG EDLTQTAPRI ALAVRQAMKN KAKDLAELYG IPKWNAAPIS 

       430        440        450        460        470        480 
QISEIYKNYL YIFNTHETKL DNIADWSYFS SIDNQVRFAR AIAYELDKNL PDISFLDSNL 

       490        500        510        520        530        540 
RKKASLIAKK IISSKKVLII SGSHVYSKSI IQASINIAIS INQKNINHVG LTFVTSSSNT 

       550        560        570        580        590        600 
LGLGILGGFS IENALKKLKN REAEAIIFME YDLYRYISKH DCDVLFKKND NIMSIDHQYT 

       610        620        630        640        650        660 
QTYKNSGFAL PSVNFTESSG TIVNFEGRAQ RFFQVYDPMF YDKKNCLYVS WKWLSFIKSK 

       670        680        690        700        710        720 
IEKKEISWIN LDNIISEYSD KYPIFKKIKT AGPNASFRVH GQKIARSPHR SSGRTALRAN 

       730        740        750        760        770        780 
INIHEPSQPK DADTMFSFSM EGYSQPNKSI SHIPFAWFPG WNSPQAWNKF QKEIGRQLIS 

       790        800        810        820        830        840 
GDSGVHLFKS NKKILDIYFH FSPKKFIKEK YWYVIPYYHI FGNEELTQYS SIIKQNIPLE 

       850        860        870        880        890        900 
YVLISELDGL ELGLKKNSIV EFNCLNQDFR LPIRLSKHLT SKHIGLPIGR KGFPISLIGE 

       910 
KVKSLWEVMS 

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References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67720.1.
RefSeqNP_660509.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9Y2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg152.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67720; AAM67720; BUsg_152.
GeneID1005350.
KEGGbas:BUsg152.
PATRIC21247085. VBIBucAph100086_0156.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1034.
KOK00336.
OMAGYGYVNR.
OrthoDBEOG6CVV7G.
ProtClustDBPRK08166.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-162-MONOMER.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR001041. 2Fe-2S_ferredoxin-type.
IPR012675. Beta-grasp_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.
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]
SUPFAMSSF54292. 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...

Entry information

Entry nameNUOG_BUCAP
AccessionPrimary (citable) accession number: Q8K9Y2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: February 19, 2014
This is version 81 of the entry and version 1 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names