Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NADH-quinone oxidoreductase subunit G

Gene

nuoG

Organism
Rickettsia conorii (strain ATCC VR-613 / Malish 7)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

NADH + quinone = NAD+ + quinol.

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster per subunit.By similarity
  • [4Fe-4S] clusterBy similarityNote: Binds 2 [4Fe-4S] clusters per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi45 – 451Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi48 – 481Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi62 – 621Iron-sulfur 1 (2Fe-2S)By similarity
Metal bindingi94 – 941Iron-sulfur 2 (4Fe-4S); via pros nitrogenBy similarity
Metal bindingi98 – 981Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi101 – 1011Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi107 – 1071Iron-sulfur 2 (4Fe-4S)By similarity
Metal bindingi146 – 1461Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi149 – 1491Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi152 – 1521Iron-sulfur 3 (4Fe-4S)By similarity
Metal bindingi196 – 1961Iron-sulfur 3 (4Fe-4S)By similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. electron carrier activity Source: InterPro
  4. metal ion binding Source: UniProtKB-KW
  5. NADH dehydrogenase (ubiquinone) activity Source: InterPro
  6. quinone binding Source: UniProtKB-KW

GO - Biological processi

  1. ATP synthesis coupled electron transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, NAD

Names & Taxonomyi

Protein namesi
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 namesi
Name:nuoG
Ordered Locus Names:RC1231
OrganismiRickettsia conorii (strain ATCC VR-613 / Malish 7)
Taxonomic identifieri272944 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group
ProteomesiUP000000816: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. membrane Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 671671NADH-quinone oxidoreductase subunit GPRO_0000118561Add
BLAST

Keywords - PTMi

Quinone

Proteomic databases

PRIDEiQ92G92.

Interactioni

Protein-protein interaction databases

STRINGi272944.RC1231.

Structurei

3D structure databases

ProteinModelPortaliQ92G92.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 78782Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini215 – 271574Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the complex I 75 kDa subunit family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 4Fe-4S Mo/W bis-MGD-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1034.
HOGENOMiHOG000031442.
KOiK00336.
OMAiNNFNTPE.
OrthoDBiEOG6CVV7G.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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.
IPR015405. NuoG_C.
[Graphical view]
PfamiPF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTiSM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR01973. NuoG. 1 hit.
PROSITEiPS51085. 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]

Sequencei

Sequence statusi: Complete.

Q92G92-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKLNVDGSE IEVSEGSTVY QACTQAGKEI PHFCYHQRLK IAGNCRMCLV
60 70 80 90 100
EMEKSPKPIA SCAMPVSNGM VIHTDTPMVK KAREGVMEFL LINHPLDCPI
110 120 130 140 150
CDQGGECNLQ DQAFRYGKGT NRFHENKRSI KDKYMGPLIK TAMTRCIQCT
160 170 180 190 200
RCIRFASDIA GIEEIGAIHR GEHIEVTSYL EQTLDSEISG NMIDICPVGA
210 220 230 240 250
LNSKPYAFKA RKWELKHTAS IGVHDAEGSN IRIDSRGDEV MRILPRVNEE
260 270 280 290 300
INEEWLSDKN RFSYDGLKYQ RLDRPYIRKN GKLVEASWSE ALKTVADKIK
310 320 330 340 350
SVKPEKIVAI AGSLSSVEAM FMLKTLLQKL GSNNYSVNQF DYKLDTMQRG
360 370 380 390 400
NYLFNTTIAG IEKADLCLLI GANPRQIAPV LNSRIGMRVR ADSLKVARIG
410 420 430 440 450
GGHNQTYKIQ DLGSDIKIIE ELAIGTHEFT KALKAAKYLM IIVGDGVYAR
460 470 480 490 500
DDGYAILSLI HKIVTEYNIM RDDWKGFNIL HNHASIVGGL DIGFNTPIKL
510 520 530 540 550
EELELAYLLG TDAIPFDKLK STFIIYQGHH GDAGASSADV ILPAAAYTEQ
560 570 580 590 600
SGIYVNLEGR PQIAEKAVSP VGVAKEDIEI IKELAGYLKI DIGMDNLQEV
610 620 630 640 650
RVRLAKEYKV FASIDRIIEN KFSKFSSKDK LSKEPITAEP INYYMTDVIS
660 670
KNSVTMAKCV EAKEARDEEV A
Length:671
Mass (Da):74,809
Last modified:May 15, 2007 - v2
Checksum:i9D9BB900EE9AE68D
GO

Sequence cautioni

The sequence AAL03769.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006914 Genomic DNA. Translation: AAL03769.1. Different initiation.
PIRiG97853.
RefSeqiNP_360868.1. NC_003103.1.

Genome annotation databases

EnsemblBacteriaiAAL03769; AAL03769; RC1231.
GeneIDi928385.
KEGGirco:RC1231.
PATRICi17889960. VBIRicCon45613_1411.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006914 Genomic DNA. Translation: AAL03769.1. Different initiation.
PIRiG97853.
RefSeqiNP_360868.1. NC_003103.1.

3D structure databases

ProteinModelPortaliQ92G92.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272944.RC1231.

Proteomic databases

PRIDEiQ92G92.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL03769; AAL03769; RC1231.
GeneIDi928385.
KEGGirco:RC1231.
PATRICi17889960. VBIRicCon45613_1411.

Phylogenomic databases

eggNOGiCOG1034.
HOGENOMiHOG000031442.
KOiK00336.
OMAiNNFNTPE.
OrthoDBiEOG6CVV7G.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 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.
IPR015405. NuoG_C.
[Graphical view]
PfamiPF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTiSM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR01973. NuoG. 1 hit.
PROSITEiPS51085. 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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC VR-613 / Malish 7.

Entry informationi

Entry nameiNUOG_RICCN
AccessioniPrimary (citable) accession number: Q92G92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 15, 2007
Last modified: January 7, 2015
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Rickettsia conorii
    (strain Malish 7): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.