NADH-quinone oxidoreductase subunit G - Rickettsia typhi (strain ATCC VR-144 / Wilmington)

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Q68VV2 (NUOG_RICTY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 59. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	RT0784

Organism

Rickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]

Taxonomic identifier

257363 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group ›

Protein attributes

Sequence length	675 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 2 4Fe-4S clusters per subunit 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 – 675

675

NADH-quinone oxidoreductase subunit G

PRO_0000287844

Regions

Domain

1 – 78

2Fe-2S ferredoxin-type

Sites

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

101

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

107

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

146

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

149

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

152

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

196

Iron-sulfur 3 (4Fe-4S) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q68VV2 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 037650EB4680CF4F
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FASTA

675

75,554

        10         20         30         40         50         60 
MIKLIIDGSE IEISEGSTVY QACIQAGKQI PHFCYHARLK IAGNCRMCLV EIEKSQKPVA 

        70         80         90        100        110        120 
SCAMPVSNGM VIHTDTSMVK KAREGVMEFL LINHPLDCPI CDQGGECDLQ DQAFRYGKGT 

       130        140        150        160        170        180 
NRFHENKRSI KDKYMGPLIK TAMTRCIQCT RCIRFANDIA GIEEIGAINR GEHMEVTSYL 

       190        200        210        220        230        240 
EQTLDSEISG NMIDICPVGA LNSKPYAFKA RKWELKHTAS IGVHDAEGSN IRIDSRADEI 

       250        260        270        280        290        300 
MRILPSVNEA INEAWISDKN RFCYDGLKYQ RLDHPYIRKN GKLVEVSWSE ALKTIMDKIK 

       310        320        330        340        350        360 
SVKPEKIAAI AGSIVSVEAM FMLKILLQKL GSNNYTVNQF NYKIDTSERG NYLFNTTIVG 

       370        380        390        400        410        420 
VEKADLCLLI GANIRQIAPI LNSRIGRRVR IGALKVVRIG IGHNQTYKIH DLGNDIKIIE 

       430        440        450        460        470        480 
DLAVGTHEYT KAFKEAKYPM IIVGDGVYGR DDGYALLSLI HKVVDKYNMM RDDWQGFNIL 

       490        500        510        520        530        540 
HNHASIVGGL DIGFNTAIKF EGVKLAYLLG ADAIPFDKLK SAFIIYQGHH GDVGAMSADV 

       550        560        570        580        590        600 
ILPSAAYTEQ SGIYVNLEGR PQIAQKAVSP VGRAKEDIEI IKEIAGYLKI DIGMDNLQEV 

       610        620        630        640        650        660 
RIRLAKEYNI FANIDKITAN RFTQFISIDK LSQEPIAARP INYYMTDVIS KNSVTMAKCV 

       670 
EAKEERKRDV AKVFY

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References

[1]

"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A.

Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017197 Genomic DNA. Translation: AAU04240.1.
RefSeq	YP_067722.1. NC_006142.1.
3D structure databases
HSSP	HSSP built from PDB template 2FUG based on UniProtKB Q56223.
ProteinModelPortal	Q68VV2.
ModBase	Search...
Protein-protein interaction databases
STRING	257363.RT0784.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAU04240; AAU04240; RT0784.
GeneID	2958618.
KEGG	rty:RT0784.
PATRIC	17910820. VBIRicTyp34752_0803.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1034.
HOGENOM	HOG000031442.
KO	K00336.
OMA	VEGGPPK.
ProtClustDB	PRK09130.
Enzyme and pathway databases
BioCyc	RTYP257363:GJEQ-824-MONOMER.
Family and domain databases
Gene3D	3.10.20.30. 1 hit.
InterPro	IPR001041. 2Fe-2S_ferredoxin-type. IPR012675. Beta-grasp_dom. IPR006656. Mopterin_OxRdtase. IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS. IPR010228. NADH_UbQ_OxRdtase_Gsu. IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. IPR015405. NuoG_C. [Graphical view]
Pfam	PF09326. DUF1982. 1 hit. PF00384. Molybdopterin. 1 hit. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
SMART	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_RICTY

Accession

Primary (citable) accession number: Q68VV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2007
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 59 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

Rickettsia typhi

Rickettsia typhi (strain Wilmington): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

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

Protein-protein interaction 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