NADH-quinone oxidoreductase subunit G - Escherichia coli (strain K12)

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P33602 (NUOG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 122. 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
NUO7

Gene names

Name:	nuoG
Ordered Locus Names:	b2283, JW2278

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	908 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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 ubiquinone. 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.
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.
Subunit structure	Composed of 13 different subunits. Subunits NuoCD, E, F, and G constitute the peripheral sector of the complex.
Subcellular location	Cytoplasm. Cell inner membrane; Peripheral membrane protein Ref.7.
Sequence similarities	Belongs to the complex I 75 kDa subunit family. Contains 1 2Fe-2S ferredoxin-type domain.
Sequence caution	The sequence BAA16111.2 differs from that shown. Reason: Erroneous initiation. The sequence CAA48366.1 differs from that shown. Reason: Frameshift at positions 715 and 806.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Cytoplasm Membrane
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro aerobic respiration Inferred from mutant phenotype. Source: EcoCyc anaerobic respiration Inferred from mutant phenotype. Source: EcoliWiki
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane respiratory chain complex I Inferred from direct assay. Source: EcoCyc
Molecular function	2 iron, 2 sulfur cluster binding Inferred from direct assay. Source: EcoCyc 4 iron, 4 sulfur cluster binding Inferred from direct assay. Source: EcoCyc NADH dehydrogenase (ubiquinone) activity Inferred from Biological aspect of Ancestor. Source: RefGenome electron carrier activity Inferred from electronic annotation. Source: InterPro molybdenum ion binding Inferred from electronic annotation. Source: InterPro oxidoreduction-driven active transmembrane transporter activity Inferred from direct assay. Source: EcoliWiki 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

Initiator methionine

Removed Ref.6

Chain

2 – 908

907

NADH-quinone oxidoreductase subunit G

PRO_0000118546

Regions

Domain

2 – 83

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

103

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

Metal binding

106

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

Metal binding

112

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

Metal binding

151

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

Metal binding

154

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

Metal binding

157

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

Metal binding

201

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

Metal binding

228

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

Metal binding

231

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

Metal binding

235

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

Metal binding

263

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

Experimental info

Sequence conflict

188

T → Q in CAA48366. Ref.1

Sequence conflict

210

T → K in CAA48366. Ref.1

Sequence conflict

390

Missing in CAA48366. Ref.1

Sequence conflict

648

S → T in CAA48366. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P33602 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 7B8626E19709D540
Show »

FASTA

908

100,299

        10         20         30         40         50         60 
MATIHVDGKE YEVNGADNLL EACLSLGLDI PYFCWHPALG SVGACRQCAV KQYQNAEDTR 

        70         80         90        100        110        120 
GRLVMSCMTP ASDGTFISID DEEAKQFRES VVEWLMTNHP HDCPVCEEGG NCHLQDMTVM 

       130        140        150        160        170        180 
TGHSFRRYRF TKRTHRNQDL GPFISHEMNR CIACYRCVRY YKDYADGTDL GVYGAHDNVY 

       190        200        210        220        230        240 
FGRPEDGTLE SEFSGNLVEI CPTGVFTDKT HSERYNRKWD MQFAPSICQQ CSIGCNISPG 

       250        260        270        280        290        300 
ERYGELRRIE NRYNGTVNHY FLCDRGRFGY GYVNLKDRPR QPVQRRGDDF ITLNAEQAMQ 

       310        320        330        340        350        360 
GAADILRQSK KVIGIGSPRA SVESNFALRE LVGEENFYTG IAHGEQERLQ LALKVLREGG 

       370        380        390        400        410        420 
IYTPALREIE SYDAVLVLGE DVTQTGARVA LAVRQAVKGK AREMAAAQKV ADWQIAAILN 

       430        440        450        460        470        480 
IGQRAKHPLF VTNVDDTRLD DIAAWTYRAP VEDQARLGFA IAHALDNSAP AVDGIEPELQ 

       490        500        510        520        530        540 
SKIDVIVQAL AGAKKPLIIS GTNAGSLEVI QAAANVAKAL KGRGADVGIT MIARSVNSMG 

       550        560        570        580        590        600 
LGIMGGGSLE EALTELETGR ADAVVVLEND LHRHASAIRV NAALAKAPLV MVVDHQRTAI 

       610        620        630        640        650        660 
MENAHLVLSA ASFAESDGTV INNEGRAQRF FQVYDPAYYD SKTVMLESWR WLHSLHSTLL 

       670        680        690        700        710        720 
SREVDWTQLD HVIDAVVAKI PELAGIKDAA PDATFRIRGQ KLAREPHRYS GRTAMRANIS 

       730        740        750        760        770        780 
VHEPRQPQDI DTMFTFSMEG NNQPTAHRSQ VPFAWAPGWN SPQAWNKFQD EVGGKLRFGD 

       790        800        810        820        830        840 
PGVRLFETSE NGLDYFTSVP ARFQPQDGKW RIAPYYHLFG SDELSQRAPV FQSRMPQPYI 

       850        860        870        880        890        900 
KLNPADAAKL GVNAGTRVSF SYDGNTVTLP VEIAEGLTAG QVGLPMGMSG IAPVLAGAHL 


EDLKEAQQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I." Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H. J. Mol. Biol. 233:109-122(1993) [PubMed: 7690854] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / AN387.
[2]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect growth on mixed amino acids." Pruss B.M., Nelms J.M., Park C., Wolfe A.J. J. Bacteriol. 176:2143-2150(1994) [PubMed: 8157582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-170.
[6]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[7]	"Protein complexes of the Escherichia coli cell envelope." Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O. J. Biol. Chem. 280:34409-34419(2005) [PubMed: 16079137] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: BL21-DE3.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X68301 Genomic DNA. Translation: CAA48366.1. Frameshift. U00096 Genomic DNA. Translation: AAC75343.2. AP009048 Genomic DNA. Translation: BAA16111.2. Different initiation. L25055 Unassigned DNA. Translation: AAA03538.1.
PIR	A65000.
RefSeq	NP_416786.4. NC_000913.2.
3D structure databases
ProteinModelPortal	P33602.
SMR	P33602. Positions 2-83.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10383N.
IntAct	P33602. 28 interactions.
MINT	MINT-1244767.
Protein family/group databases
TCDB	3.D.1.1.1. H+ or Na+-translocating NADH dehydrogenase (NDH) family.
Proteomic databases
PRIDE	P33602.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000004081; EBESCP00000004081; EBESCG00000003333. EBESCT00000004082; EBESCP00000004082; EBESCG00000003333. EBESCT00000017737; EBESCP00000017028; EBESCG00000016793.
GeneID	946762.
GenomeReviews	Gene locus JW2278 in contig AP009048_GR. Gene locus b2283 in contig U00096_GR.
KEGG	ecj:JW2278. eco:b2283.
PATRIC	32119933. VBIEscCol129921_2376.
Organism-specific databases
EchoBASE	EB2011.
EcoGene	EG12087. nuoG.
Phylogenomic databases
eggNOG	COG1034.
GeneTree	EBGT00050000011361.
HOGENOM	HBG488172.
OMA	PSICHGC.
PhylomeDB	P33602.
ProtClustDB	PRK08166.
Enzyme and pathway databases
BioCyc	EcoCyc:NUOG-MONOMER. MetaCyc:NUOG-MONOMER.
Gene expression databases
Genevestigator	P33602.
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. PF04879. Molybdop_Fe4S4. 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_ECOLI

Accession

Primary (citable) accession number: P33602
Secondary accession number(s): P76489, P78184, P78185

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 122 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents