O67386 (NUOI2_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NADH-quinone oxidoreductase subunit I 2
EC=1.6.99.5

Alternative name(s):
NADH dehydrogenase I subunit I 2
NDH-1 subunit I 2

Gene names

Name:	nuoI2
Ordered Locus Names:	aq_1375

Organism

Aquifex aeolicus (strain VF5)

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	208 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 – 208	208	NADH-quinone oxidoreductase subunit I 2 HAMAP MF_01351		PRO_0000298479
Regions
	Domain	79 – 109	31	4Fe-4S ferredoxin-type 1
	Domain	119 – 148	30	4Fe-4S ferredoxin-type 2
Sites
	Metal binding	88	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	91	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	94	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	98	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	128	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	131	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	134	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	138	1	Iron-sulfur 1 (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O67386 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 5500203BFD4863B2	FASTA	208	24,572
	10 20 30 40 50 60 MIKKVAAKPL SWLERIFFID FIKGLRITLK NALRKTITTH YPYEKITPPK RFRGYFAHKV 70 80 90 100 110 120 VDGTEPQPAF QEWVNRYNIL VEYGKSRCVV CLRCKRACPV PQLFEIEGKK LPNGKRVVSV 130 140 150 160 170 180 FNMNMLLCTY CGFCVDACPV DCLYQTDIHE NASYTRKDAV LTLEILEQIG RDWQRRRERE 190 200 PDRIWIDDEQ RMKLWGENNV KLPKPEEV

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: AAC07349.1.
PIR	G70419.
RefSeq	NP_213950.1. NC_000918.1.
3D structure databases
ProteinModelPortal	O67386.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1192916.
GenomeReviews	Gene locus aq_1375 in contig AE000657_GR.
KEGG	aae:aq_1375.
NMPDR	fig|224324.1.peg.965.
PATRIC	20959926. VBIAquAeo85532_1077.
Phylogenomic databases
HOGENOM	HBG724359.
OMA	QWEVEIS.
PhylomeDB	O67386.
ProtClustDB	CLSK2459820.
Enzyme and pathway databases
BioCyc	AAEO224324:AQ_1375-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. 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]
PROSITE	PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUOI2_AQUAE

Accession

Primary (citable) accession number: O67386

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program