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Protein

NADH-quinone oxidoreductase subunit G

Gene

nuoG

Organism
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi)
Status
Reviewed-Annotation score: -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 + a quinone = NAD+ + a 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)DescriptionActionsGraphical viewLength
Metal bindingi34Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi45Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi48Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi62Iron-sulfur 1 (2Fe-2S)By similarity1
Metal bindingi94Iron-sulfur 2 (4Fe-4S); via tele nitrogenPROSITE-ProRule annotation1
Metal bindingi98Iron-sulfur 2 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi101Iron-sulfur 2 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi107Iron-sulfur 2 (4Fe-4S)PROSITE-ProRule annotation1
Metal bindingi146Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi149Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi152Iron-sulfur 3 (4Fe-4S)By similarity1
Metal bindingi196Iron-sulfur 3 (4Fe-4S)By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Ligand2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
NADH-quinone oxidoreductase subunit G (EC:1.6.5.11)
Alternative name(s):
NADH dehydrogenase I subunit G
NDH-1 subunit G
Gene namesi
Name:nuoG
Ordered Locus Names:RF_1262
OrganismiRickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi)
Taxonomic identifieri315456 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group
Proteomesi
  • UP000008548 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002878431 – 671NADH-quinone oxidoreductase subunit GAdd BLAST671

Keywords - PTMi

Quinone

Proteomic databases

PRIDEiQ4UK22

Interactioni

Protein-protein interaction databases

STRINGi315456.RF_1262

Structurei

3D structure databases

ProteinModelPortaliQ4UK22
SMRiQ4UK22
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 782Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST78
Domaini78 – 1174Fe-4S His(Cys)3-ligated-typePROSITE-ProRule annotationAdd BLAST40
Domaini215 – 2714Fe-4S Mo/W bis-MGD-typePROSITE-ProRule annotationAdd BLAST57

Sequence similaritiesi

Belongs to the complex I 75 kDa subunit family.Curated

Phylogenomic databases

eggNOGiENOG4108IEH Bacteria
COG1034 LUCA
HOGENOMiHOG000031442
KOiK00336
OMAiPQASCAM
OrthoDBiPOG091H09JF

Family and domain databases

CDDicd00207 fer2, 1 hit
InterProiView protein in InterPro
IPR036010 2Fe-2S_ferredoxin-like_sf
IPR001041 2Fe-2S_ferredoxin-type
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
PfamiView protein in Pfam
PF00384 Molybdopterin, 1 hit
PF10588 NADH-G_4Fe-4S_3, 1 hit
PF09326 NADH_dhqG_C, 1 hit
SMARTiView protein in SMART
SM00929 NADH-G_4Fe-4S_3, 1 hit
SUPFAMiSSF54292 SSF54292, 1 hit
TIGRFAMsiTIGR01973 NuoG, 1 hit
PROSITEiView protein in PROSITE
PS51085 2FE2S_FER_2, 1 hit
PS51839 4FE4S_HC3, 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

Sequencei

Sequence statusi: Complete.

Q4UK22-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIKLNIDGSE IEVSEGSTVY QACTQAGKEI PHFCYHERLK IAGNCRMCLV
60 70 80 90 100
EMEKSPKPIA SCAMPVSNGM VIHTDTPMVK KAREGVMEFL LINHPLDCPI
110 120 130 140 150
CDQGGECDLQ DQAFRYGKGT NRFHENKRSI KDKYMGPLIK TAMTRCIQCT
160 170 180 190 200
RCIRFANDIA GIEEMGAIHR GEHMEVTSYL EQTLDSEMSG NMIDICPVGA
210 220 230 240 250
LNSKPYAFKA RKWELKHTAS IGVHDAEGSN IRIDSRGDEV MRILPRVNEE
260 270 280 290 300
INEEWLSDKN RFSYDGLKYQ RLDLPYIRKN GKLVEASWSE ALKTIADKIK
310 320 330 340 350
SVKPEKIAAI AGSLVSVEAM FMLKTLLQKL GSNNYSVNQF DYKFDTTQRG
360 370 380 390 400
NYLFNTTIAG VEKADLCLLI GANLRQIAPV LNSRIGQRVR AGSLKVARIG
410 420 430 440 450
EGHNQTYRIQ DLGSDIKIIE ELAIGTHEFT KALKAAKYPM IIVGDGVYAR
460 470 480 490 500
DDGYAILSLI HKIVAEYNIM RDDFQGFNML HNHASIVGGL DIGFNTPIKL
510 520 530 540 550
EELELTYLLG ADELPFDKLK SAFIIYQGHH GDSGAANADV ILPAAAYTEQ
560 570 580 590 600
SGIYVNLEGR PQIAEKAVAP VGVAKEDIEI IKELAGSLKI DIGMDNLQEV
610 620 630 640 650
RVRLAKEYKI FANIDKIVES KFAKFSFKDK LSKEPITMGP INYYMTDVIS
660 670
KNSVTMAKCV EAKEKRNERA A
Length:671
Mass (Da):74,861
Last modified:July 5, 2005 - v1
Checksum:i8ABAC83059DD6C01
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000053 Genomic DNA Translation: AAY62113.1
RefSeqiWP_011271562.1, NC_007109.1

Genome annotation databases

EnsemblBacteriaiAAY62113; AAY62113; RF_1262
KEGGirfe:RF_1262

Similar proteinsi

Entry informationi

Entry nameiNUOG_RICFE
AccessioniPrimary (citable) accession number: Q4UK22
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: July 5, 2005
Last modified: May 23, 2018
This is version 86 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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