NADH-quinone oxidoreductase subunit G

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P59962 (NUOG_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. History...

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

Documents (1) |

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:	Mb3175

Organism

Mycobacterium bovis [Complete proteome] [HAMAP]

Taxonomic identifier

1765 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	806 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. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. 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.
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 molybdenum ion binding Inferred from electronic annotation. Source: InterPro 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 – 806

806

NADH-quinone oxidoreductase subunit G

PRO_0000118558

Regions

Domain

15 – 93

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

111

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

Metal binding

115

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

Metal binding

118

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

Metal binding

124

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

Metal binding

164

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

Metal binding

167

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

Metal binding

170

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

Metal binding

214

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

Metal binding

240

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

243

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

247

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

275

Iron-sulfur 4 (4Fe-4S) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

P59962 [UniParc].

Last modified October 31, 2003. Version 1.
Checksum: D674D74FA6FF3E81
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FASTA

806

85,412

        10         20         30         40         50         60 
MTQAADTDIR VGQPEMVTLT IDGVEISVPK GTLVIRAAEL MGIQIPRFCD HPLLEPVGAC 

        70         80         90        100        110        120 
RQCLVEVEGQ RKPLASCTTV ATDDMVVRTQ LTSEIADKAQ HGVMELLLIN HPLDCPMCDK 

       130        140        150        160        170        180 
GGECPLQNQA MSNGRTDSRF TEAKRTFAKP INISAQVLLD RERCILCARC TRFSDQIAGD 

       190        200        210        220        230        240 
PFIDMQERGA LQQVGIYADE PFESYFSGNT VQICPVGALT GTAYRFRARP FDLVSSPSVC 

       250        260        270        280        290        300 
EHCASGCAQR TDHRRGKVLR RLAGDDPEVN EEWNCDKGRW AFTYATQPDV ITTPLIRDGG 

       310        320        330        340        350        360 
DPKGALVPTS WSHAMAVAAQ GLAAARGRTG VLVGGRVTWE DAYAYAKFAR ITLGTNDIDF 

       370        380        390        400        410        420 
RARPHSAEEA DFLAARIAGR HMAVSYADLE SAPVVLLVGF EPEDESPIVF LRLRKAARRH 

       430        440        450        460        470        480 
RVPVYTIAPF ATGGLHKMSG RLIKTVPGGE PAALDDLATG AVGDLLATPG AVIMVGERLA 

       490        500        510        520        530        540 
TVPGGLSAAA RLADTTGARL AWVPRRAGER GALEAGALPT LLPGGRPLAD EVARAQVCAA 

       550        560        570        580        590        600 
WHIAELPAAA GRDADGILAA AADETLAALL VGGIEPADFA DPDAVLAALD ATGFVVSLEL 

       610        620        630        640        650        660 
RHSAVTERAD VVFPVAPTTQ KAGAFVNWEG RYRTFEPALR GSTLQAGQSD HRVLDALADD 

       670        680        690        700        710        720 
MGVHLGVPTV EAAREELAAL GIWDGKHAAG PHIAATGPTQ PEAGEAILTG WRMLLDEGRL 

       730        740        750        760        770        780 
QDGEPYLAGT ARTPVVRLSP DTAAEIGAAD GEAVTVSTSR GSITLPCSVT DMPDRVVWLP 

       790        800 
LNSAGSTVHR QLRVTIGSIV KIGAGS

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References

[1]

"The complete genome sequence of Mycobacterium bovis."
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.

Hewinson R.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248345 Genomic DNA. Translation: CAD95267.1.
RefSeq	NP_856820.1. NC_002945.3.
3D structure databases
ProteinModelPortal	P59962.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000016747; EBMYCP00000016582; EBMYCG00000016742.
GeneID	1093502.
GenomeReviews	Gene locus Mb3175 in contig BX248333_GR.
KEGG	mbo:Mb3175.
PATRIC	18008728. VBIMycBov88188_3493.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000015815.
HOGENOM	HBG715033.
OMA	CRQCLVD.
ProtClustDB	PRK07860.
Enzyme and pathway databases
BioCyc	MBOV233413:MB3175-MONOMER.
Family and domain databases
InterPro	IPR009010. Asp_de-COase-like_fold. IPR012675. Beta-grasp_ferredoxin-type. IPR001041. Ferredoxin. IPR006657. MoPterin_dinucl-bd_dom. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4_dom. IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS. IPR010228. NADH_UbQ_OxRdtase_Gsu. IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. [Graphical view]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
KO	K00336.
Pfam	PF00111. Fer2. 1 hit. PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
SMART	SM00926. Molybdop_Fe4S4. 1 hit. SM00929. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit. 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_MYCBO

Accession

Primary (citable) accession number: P59962

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	October 31, 2003
Last modified:	January 25, 2012
This is version 64 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

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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents