Skip Header

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

Q1RKD2

- NUOG_RICBR

UniProt

Q1RKD2 - NUOG_RICBR

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

NADH-quinone oxidoreductase subunit G

Gene

nuoG

Organism
Rickettsia bellii (strain RML369-C)
Status
Reviewed - 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

Enzyme and pathway databases

BioCyciRBEL336407:GJCY-103-MONOMER.

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:RBE_0101
OrganismiRickettsia bellii (strain RML369-C)
Taxonomic identifieri336407 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group
ProteomesiUP000001951: Chromosome

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 681681NADH-quinone oxidoreductase subunit GPRO_0000287842Add
BLAST

Keywords - PTMi

Quinone

Proteomic databases

PRIDEiQ1RKD2.

Interactioni

Protein-protein interaction databases

STRINGi336407.RBE_0101.

Structurei

3D structure databases

ProteinModelPortaliQ1RKD2.
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.
OMAiFQGNDVA.
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.

Q1RKD2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIKLTIDGQE IEVSEGTTVY QACTKAGKEI PHFCYHERLK IAGNCRMCLV
60 70 80 90 100
EMEKSPKPIA SCAMPVGNGM VIHTDTPMVK KAREGVMEFL LVNHPLDCPI
110 120 130 140 150
CDQGGECDLQ DQAFRYGKGT NRFHENKRSI KDKYMGPLIK TAMTRCIQCT
160 170 180 190 200
RCIRFANDIA GIEEMGAIHR GEHMEVTSYL EQTLDSEISG NMIDICPVGA
210 220 230 240 250
LNSKPYAFKA RKWELRHTAS IGVHDAEGSN IRIDSRGDEV MRVLPRVNEE
260 270 280 290 300
INEEWLSDKN RFSYDGLKYQ RLDQPYIRKN GKLVSASWDE ALKAIADKIK
310 320 330 340 350
SIKPEKITAF AGTLASVEAM FMLKTFLQKI GCNNYNVNQF DYKLDTTQRG
360 370 380 390 400
NYLFNTTIAG LEKADLCLLI GANPRQIAPV LNSRIGGRVR AGSLKVARIG
410 420 430 440 450
EGHNQTYKIQ DLGSDLKILE ELALDEHKFA EELKAAKYPI IIVGDGVYGR
460 470 480 490 500
NDGHAILSLI HKIVDKYNIM RDDWKGFNIL HNHASMVGGF DIGFDTSLGK
510 520 530 540 550
LEDIELAYLL GADELPFDKL KSAFIVYQGH HGDIGATKAD IILPSAAYTE
560 570 580 590 600
QSGIYVNLEG RPQIAEKAVS PVGKAKEDIA IIKELADCLK LDTLVSNLQE
610 620 630 640 650
IRTKLAKEYP IFANIGKIID NKFAKFSSKD KLSKEPITAE TINYYMTDVI
660 670 680
SKNSVTMARC VEAKQEMSSR GLSTGSRKKR E
Length:681
Mass (Da):76,012
Last modified:May 16, 2006 - v1
Checksum:i6DC4D413820168B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000087 Genomic DNA. Translation: ABE04182.1.
RefSeqiYP_537271.1. NC_007940.1.

Genome annotation databases

EnsemblBacteriaiABE04182; ABE04182; RBE_0101.
GeneIDi3995635.
KEGGirbe:RBE_0101.
PATRICi17881458. VBIRicBel102610_0113.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000087 Genomic DNA. Translation: ABE04182.1 .
RefSeqi YP_537271.1. NC_007940.1.

3D structure databases

ProteinModelPortali Q1RKD2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 336407.RBE_0101.

Proteomic databases

PRIDEi Q1RKD2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABE04182 ; ABE04182 ; RBE_0101 .
GeneIDi 3995635.
KEGGi rbe:RBE_0101.
PATRICi 17881458. VBIRicBel102610_0113.

Phylogenomic databases

eggNOGi COG1034.
HOGENOMi HOG000031442.
KOi K00336.
OMAi FQGNDVA.
OrthoDBi EOG6CVV7G.

Enzyme and pathway databases

BioCyci RBEL336407:GJCY-103-MONOMER.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR001041. 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 ]
Pfami PF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view ]
SMARTi SM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view ]
SUPFAMi SSF54292. SSF54292. 1 hit.
TIGRFAMsi TIGR01973. NuoG. 1 hit.
PROSITEi PS51085. 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 ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
    Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
    PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RML369-C.

Entry informationi

Entry nameiNUOG_RICBR
AccessioniPrimary (citable) accession number: Q1RKD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 16, 2006
Last modified: November 26, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Rickettsia bellii strain RML369-C
    Rickettsia bellii (strain RML369-C): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3