P57259 (NUOI_BUCAI) 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:	BU161

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)

Taxonomic identifier

107806 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	180 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 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex By similarity.
Subcellular location	Cell 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 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 – 180	180	NADH-quinone oxidoreductase subunit I HAMAP MF_01351		PRO_0000118726
Regions
	Domain	50 – 80	31	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)
	P57259 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: AF9FC8B6A7229A33	FASTA	180	20,660
	10 20 30 40 50 60 MTLKNIIIGF FTQIRSIFMI GANIFSKPET KLYPEEKVYL APRYRGRIIL TRNIDGQERC 70 80 90 100 110 120 VACNLCAVVC PVDCISLQKS EKTDGRWYPK FFRINFSRCI FCGLCEEACP TAAIQLMPDF 130 140 150 160 170 180 ELSDFKRQDL VYEKKDLLIS GPGKYPNYDF YNFSGVTLKG KKTGDLEIQA RPIDVKDLLP

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: APS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000003 Genomic DNA. Translation: BAB12879.1.
RefSeq	NP_239993.1. NC_002528.1.
3D structure databases
ProteinModelPortal	P57259.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000003093; EBBUCP00000002869; EBBUCG00000003093.
GeneID	1109605.
GenomeReviews	Gene locus BU161 in contig BA000003_GR.
KEGG	buc:BU161.
PATRIC	21243838. VBIBucAph127364_0171.
Phylogenomic databases
GeneTree	EBGT00050000007927.
HOGENOM	HBG724359.
OMA	RYWSVAG.
PhylomeDB	P57259.
ProtClustDB	PRK05888.
Enzyme and pathway databases
BioCyc	BSP107806:BU161-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	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_BUCAI

Accession

Primary (citable) accession number: P57259

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	January 25, 2012
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program