Q8XCX2 (NUOG_ECO57) Reviewed, UniProtKB/Swiss-Prot

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:	Z3542, ECs3167

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [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	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 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 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.
Subunit structure	Composed of 13 different subunits. Subunits NuoCD, E, F, and G constitute the peripheral sector of the complex.
Sequence similarities	Belongs to the complex I 75 kDa subunit family. Contains 1 2Fe-2S ferredoxin-type domain.
Sequence caution	The sequence AAG57412.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB36590.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 908	907	NADH-quinone oxidoreductase subunit G		PRO_0000118547
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) Potential
	Metal binding	231	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	235	1	Iron-sulfur 4 (4Fe-4S) Potential
	Metal binding	263	1	Iron-sulfur 4 (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8XCX2 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 048222FD1B9230CD	FASTA	908	100,303
	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 LHRHASATRV 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 FQCRMPQPYI 850 860 870 880 890 900 KLNPADAAKL GVNAGTRVSF SYDGNTVTLP VEIAEGLTAG QVGLPMGMSG IAPVLAGAHL EDLKEAQQ

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG57412.1. Different initiation. BA000007 Genomic DNA. Translation: BAB36590.1. Different initiation.
PIR	G91024. H85868.
RefSeq	NP_288857.1. NC_002655.2. NP_311194.2. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8XCX2.
SMR	Q8XCX2. Positions 2-83.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000025111; EBESCP00000024004; EBESCG00000024165. EBESCT00000058468; EBESCP00000056296; EBESCG00000057516.
GeneID	916875. 957432.
GenomeReviews	Gene locus Z3542 in contig AE005174_GR. Gene locus ECs3167 in contig BA000007_GR.
KEGG	ece:Z3542. ecs:ECs3167.
PATRIC	18355720. VBIEscCol44059_3061.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000011361.
HOGENOM	HBG488172.
OMA	PSICHGC.
ProtClustDB	PRK08166.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3167-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. 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_ECO57

Accession

Primary (citable) accession number: Q8XCX2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 68 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program