Reviewed, UniProtKB/Swiss-Prot P33602 (NUOG_ECOLI)

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) [Complete proteome] [HAMAP]

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 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
Gene Ontology (GO)
Biological process	ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 iron 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
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 908	907	NADH-quinone oxidoreductase subunit G		PRO_0000118546
Regions
	Domain	2 – 83	82	2Fe-2S ferredoxin-type
Sites
	Metal binding	34	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	45	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	48	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	67	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	99	1	Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
	Metal binding	103	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	106	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	112	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	151	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	154	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	157	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	201	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	228	1	Iron-sulfur 4 (4Fe-4S) By similarity
	Metal binding	231	1	Iron-sulfur 4 (4Fe-4S) By similarity
	Metal binding	235	1	Iron-sulfur 4 (4Fe-4S) By similarity
	Metal binding	263	1	Iron-sulfur 4 (4Fe-4S) By similarity
Experimental info
	Sequence conflict	188	1	T → Q in CAA48366. Ref.1
	Sequence conflict	210	1	T → K in CAA48366. Ref.1
	Sequence conflict	390	1	Missing in CAA48366. Ref.1
	Sequence conflict	648	1	S → T in CAA48366. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P33602-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 7B8626E19709D540	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

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. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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	AP_002881.1. NP_416786.4.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:10383N.
IntAct	P33602. 28 interactions.
Protein family/group databases
TCDB	3.D.1.1.1. proton-translocating NADH dehydrogenase (NDH) family.
Genome annotation databases
GeneID	946762.
GenomeReviews	Gene locus JW2278 in contig AP009048_GR. Gene locus b2283 in contig U00096_GR.
KEGG	ecj:JW2278. eco:b2283.
Organism-specific databases
EchoBASE	EB2011.
EcoGene	EG12087. nuoG.
CMR	Search...
Phylogenomic databases
HOGENOM	P33602.
OMA	P33602. EVGGHLR.
Enzyme and pathway databases
BioCyc	EcoCyc:NUOG-MON. MetaCyc:NUOG-MON.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR009010. Asp_de-COase-like_fold. IPR001041. Ferredoxin. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4. 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.
Pfam	PF00111. Fer2. 1 hit. PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
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:	June 16, 2009
This is version 98 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)