Reviewed, UniProtKB/Swiss-Prot Q92G92 (NUOG_RICCN)

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:	RC1231

Organism

Rickettsia conorii [Complete proteome] [HAMAP]

Taxonomic identifier

781 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group

Protein attributes

Sequence length	671 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 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
	Chain	1 – 671	671	NADH-quinone oxidoreductase subunit G		PRO_0000118561
Regions
	Domain	1 – 78	78	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	62	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	94	1	Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
	Metal binding	98	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	101	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	107	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	146	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	149	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	152	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	196	1	Iron-sulfur 3 (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92G92-1 [UniParc]. Last modified May 15, 2007. Version 2. Checksum: 9D9BB900EE9AE68D	FASTA	671	74,809
	10 20 30 40 50 60 MIKLNVDGSE IEVSEGSTVY QACTQAGKEI PHFCYHQRLK IAGNCRMCLV EMEKSPKPIA 70 80 90 100 110 120 SCAMPVSNGM VIHTDTPMVK KAREGVMEFL LINHPLDCPI CDQGGECNLQ DQAFRYGKGT 130 140 150 160 170 180 NRFHENKRSI KDKYMGPLIK TAMTRCIQCT RCIRFASDIA GIEEIGAIHR GEHIEVTSYL 190 200 210 220 230 240 EQTLDSEISG NMIDICPVGA LNSKPYAFKA RKWELKHTAS IGVHDAEGSN IRIDSRGDEV 250 260 270 280 290 300 MRILPRVNEE INEEWLSDKN RFSYDGLKYQ RLDRPYIRKN GKLVEASWSE ALKTVADKIK 310 320 330 340 350 360 SVKPEKIVAI AGSLSSVEAM FMLKTLLQKL GSNNYSVNQF DYKLDTMQRG NYLFNTTIAG 370 380 390 400 410 420 IEKADLCLLI GANPRQIAPV LNSRIGMRVR ADSLKVARIG GGHNQTYKIQ DLGSDIKIIE 430 440 450 460 470 480 ELAIGTHEFT KALKAAKYLM IIVGDGVYAR DDGYAILSLI HKIVTEYNIM RDDWKGFNIL 490 500 510 520 530 540 HNHASIVGGL DIGFNTPIKL EELELAYLLG TDAIPFDKLK STFIIYQGHH GDAGASSADV 550 560 570 580 590 600 ILPAAAYTEQ SGIYVNLEGR PQIAEKAVSP VGVAKEDIEI IKELAGYLKI DIGMDNLQEV 610 620 630 640 650 660 RVRLAKEYKV FASIDRIIEN KFSKFSSKDK LSKEPITAEP INYYMTDVIS KNSVTMAKCV 670 EAKEARDEEV A

References

[1]

"Mechanisms of evolution in Rickettsia conorii and R. prowazekii." Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D. Science 293:2093-2098(2001) [PubMed: 11557893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE006914 Genomic DNA. Translation: AAL03769.1. Different initiation.
PIR	G97853.
RefSeq	NP_360868.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	928385.
GenomeReviews	Gene locus RC1231 in contig AE006914_GR.
KEGG	rco:RC1231.
NMPDR	fig|272944.1.peg.1231.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q92G92.
Enzyme and pathway databases
BioCyc	RCON272944:RC1231-MON.
BRENDA	1.6.99.5. 267518.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR012675. b-grasp_ferredoxin-like. IPR001041. Ferredoxin. 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]
Gene3D	G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF09326. DUF1982. 1 hit. PF00111. Fer2. 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_RICCN

Accession

Primary (citable) accession number: Q92G92

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	May 15, 2007
Last modified:	June 16, 2009
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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