Q57DU3 (NUOI_BRUAB) Reviewed, UniProtKB/Swiss-Prot

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:	BruAb1_0824

Organism

Brucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]

Taxonomic identifier

262698 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella abortus › Brucella abortus bv. 1

Protein attributes

Sequence length	163 AA.
Sequence status	Complete.
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. HAMAP-Rule MF_01351
Catalytic activity	NADH + quinone = NAD+ + quinol. HAMAP-Rule 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 HAMAP-Rule MF_01351.
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	photosynthesis, light reaction Inferred from electronic annotation. Source: HAMAP
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (quinone) activity Inferred from electronic annotation. Source: HAMAP 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 – 163	163	NADH-quinone oxidoreductase subunit I HAMAP-Rule MF_01351		PRO_0000250883
Regions
	Domain	53 – 83	31	4Fe-4S ferredoxin-type 1
	Domain	94 – 123	30	4Fe-4S ferredoxin-type 2
Sites
	Metal binding	63	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	66	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	69	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	73	1	Iron-sulfur 2 (4Fe-4S) 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	109	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	113	1	Iron-sulfur 1 (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q57DU3 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: D9F30BE81CF5CD3F	FASTA	163	18,519
	10 20 30 40 50 60 MASIAQAAKS LLLKEFASAF ALSMRQFFAP KATLNYPHEK GPVSPRFRGE HALRRYPNGE 70 80 90 100 110 120 ERCIACKLCE AICPAQAITI EAGPRRNDGT RRTVRYDIDM VKCIYCGFCQ EACPVDAIVE 130 140 150 160 GPNFEFATET REELYYDKDK LLANGDRWER EIARNIAMDA PYR

References

[1]

"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017223 Genomic DNA. Translation: AAX74191.1.
RefSeq	YP_221552.1. NC_006932.1.
3D structure databases
HSSP	HSSP built from PDB template 2FDN based on UniProtKB P00198.
ProteinModelPortal	Q57DU3.
ModBase	Search...
Protein-protein interaction databases
STRING	262698.BruAb1_0824.
Proteomic databases
PRIDE	Q57DU3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAX74191; AAX74191; BruAb1_0824.
GeneID	3340892.
KEGG	bmb:BruAb1_0824.
PATRIC	17823272. VBIBruAbo15061_0867.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1143.
HOGENOM	HOG000228289.
KO	K00338.
OMA	CPAMAIT.
ProtClustDB	PRK05888.
Enzyme and pathway databases
BioCyc	BABO262698:GJC2-836-MONOMER.
Family and domain databases
Gene3D	1.10.1060.10. 1 hit.
HAMAP	MF_01351. NDH1_NuoI.
InterPro	IPR001450. 4Fe4S-bd_dom. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR012285. Fum_reductase_C. IPR010226. NADH_quinone_OxRdtase_chainI. [Graphical view]
Pfam	PF12838. Fer4_7. 1 hit. [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_BRUAB

Accession

Primary (citable) accession number: Q57DU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program