O67337 (NUOI1_AQUAE) 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:	aq_1317

Organism

Aquifex aeolicus (strain VF5)

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	201 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 MF_01351
Catalytic activity	NADH + quinone = NAD+ + quinol. HAMAP MF_01351
Cofactor	Binds 2 4Fe-4S clusters per subunit By similarity. HAMAP MF_01351
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 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 Reference proteome
Gene Ontology (GO)
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: EC electron carrier activity Inferred from electronic annotation. Source: InterPro metal 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 – 201	201	NADH-quinone oxidoreductase subunit I HAMAP MF_01351		PRO_0000250875
Regions
	Domain	78 – 107	30	4Fe-4S ferredoxin-type 1
	Domain	116 – 147	32	4Fe-4S ferredoxin-type 2
Sites
	Metal binding	87	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	90	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	93	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	97	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	127	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	130	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	133	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	137	1	Iron-sulfur 1 (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O67337 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 6A73F63A3ABCDE07	FASTA	201	23,410
	10 20 30 40 50 60 MGVKKLSRKD YLNILESILF IDFLKGLSVT LKNLLRRPIT TEYPKEKLTP PKRFRGAHGH 70 80 90 100 110 120 YVWDGTEPDS LKAIEKFMSY EKAKSRCVAC YMCQTACPMP TLFRIEAVQL PNGKKKVVRF 130 140 150 160 170 180 DMNLLNCLFC GLCVDACPVG CLTMTDIFEL ANYSRRNEVL RMEDLEKFAI DFKQRRGNEP 190 200 DRIWPNDEER EKLWGKIEWS G

References

[1]

"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000657 Genomic DNA. Translation: AAC07300.1.
PIR	F70413.
RefSeq	NP_213901.1. NC_000918.1.
3D structure databases
ProteinModelPortal	O67337.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1192775.
GenomeReviews	Gene locus aq_1317 in contig AE000657_GR.
KEGG	aae:aq_1317.
NMPDR	fig|224324.1.peg.916.
PATRIC	20959816. VBIAquAeo85532_1025.
Phylogenomic databases
HOGENOM	HBG724359.
OMA	PCDCIEV.
PhylomeDB	O67337.
ProtClustDB	CLSK233603.
Enzyme and pathway databases
BioCyc	AAEO224324:AQ_1317-MONOMER.
Family and domain databases
HAMAP	MF_01351. NDH1_NuoI. [Tree]
InterPro	IPR001450. 4Fe4S-bd_dom. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR012285. Fum_reductase_C. IPR009051. Helical_ferredxn. IPR010226. NADH_quinone_OxRdtase_chainI. [Graphical view]
Gene3D	G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
KO	K00338.
Pfam	PF00037. Fer4. 1 hit. [Graphical view]
SUPFAM	SSF46548. Helical_ferredxn. 1 hit.
PROSITE	PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUOI1_AQUAE

Accession

Primary (citable) accession number: O67337

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program