Reviewed, UniProtKB/Swiss-Prot Q1RKD0 (NUOI_RICBR)

Names and origin

Protein names

Recommended name:
    NADH-quinone oxidoreductase subunit I
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I subunit I
    NDH-1 subunit I

Gene names

Name:	nuoI
Ordered Locus Names:	RBE_0103

Organism

Rickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]

Taxonomic identifier

336407 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia

Protein attributes

Sequence length	159 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. 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. HAMAP MF_01351
Cofactor	Binds 2 4Fe-4S clusters per subunit By similarity.
Subunit structure	NDH-1 is composed of 14 different subunits. Subunits nuoA, H, J, K, L, M, N constitute the membrane sector of the complex By similarity.
Subcellular location	Cell inner membrane; Peripheral membrane protein Potential.
Sequence similarities	Belongs to the complex I 23 kDa subunit family. Contains 2 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Repeat
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: HAMAP photosynthesis, light reaction Inferred from electronic annotation. Source: HAMAP
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (quinone) activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: HAMAP 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 – 159	159	NADH-quinone oxidoreductase subunit I HAMAP MF_01351		PRO_0000245736
Regions
	Domain	51 – 80	30	4Fe-4S ferredoxin-type 1
	Domain	90 – 119	30	4Fe-4S ferredoxin-type 2
Sites
	Metal binding	60	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	63	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	66	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	70	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	99	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	102	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	105	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	109	1	Iron-sulfur 1 (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1RKD0-1 [UniParc]. Last modified May 16, 2006. Version 1. Checksum: 98D4E4F7916A004A	FASTA	159	18,526
	10 20 30 40 50 60 MINYLKSFFL YEIIRGLALT LKYFFKAKVT INYPYEKSPV SPRFKGEHAL RRYENGEERC 70 80 90 100 110 120 IACKLCEAIC PAQAIVIEAD EREDGSRRTT RYDIDMTKCI YCGLCQEACP VDAIVEGPNF 130 140 150 EFASLTHTAL IYDKEKLLQN GDRWEQALAN KLHKDYEYR

References

[1]

"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens." Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D. PLoS Genet. 2:733-744(2006) [PubMed: 16703114] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000087 Genomic DNA. Translation: ABE04184.1.
RefSeq	YP_537273.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q1RKD0.
Genome annotation databases
GeneID	3995637.
GenomeReviews	Gene locus RBE_0103 in contig CP000087_GR.
KEGG	rbe:RBE_0103.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1RKD0.
OMA	NYPYEKG
Enzyme and pathway databases
BioCyc	RBEL336407:RBE_0103-MON.
Family and domain databases
HAMAP	MF_01351. [Tree]
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR001450. 4Fe4S_Fe_S_bd_subgr. IPR017900. 4Fe4S_Fe_S_CS. IPR009051. Helical_ferredxn. IPR010226. NADH_quinone_OxRdtase_chainI. [Graphical view]
Pfam	PF00037. Fer4. 2 hits. [Graphical view]
TIGRFAMs	TIGR01971. NuoI. 1 hit.
PROSITE	PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUOI_RICBR

Accession

Primary (citable) accession number: Q1RKD0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	May 16, 2006
Last modified:	November 24, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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