Q98KR4 (NUOI_RHILO) 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:	mll1359

Organism

Rhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]

Taxonomic identifier

266835 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Phyllobacteriaceae › Mesorhizobium

Protein attributes

Sequence length	164 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
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 – 164	164	NADH-quinone oxidoreductase subunit I HAMAP MF_01351		PRO_0000250931
Regions
	Domain	54 – 84	31	4Fe-4S ferredoxin-type 1
	Domain	95 – 124	30	4Fe-4S ferredoxin-type 2
Sites
	Metal binding	64	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	67	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	70	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	74	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	104	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	107	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	110	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	114	1	Iron-sulfur 1 (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q98KR4 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 08411692867497B1	FASTA	164	18,812
	10 20 30 40 50 60 MMSALSQAAK SLLLQDFVSA FFLSMRQFFA PKETINYPHE KGPVSPRFRG EHALRRYPNG 70 80 90 100 110 120 EERCIACKLC EAICPAQAIT IEAGPRRNDG TRRTVRYDID MVKCIYCGFC QEACPVDAIV 130 140 150 160 EGPNFEFATE TREELYYDKD KLLANGDRWE RELARNISLD APYR

References

[1]

"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti." Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S. DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MAFF303099.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000012 Genomic DNA. Translation: BAB48750.1.
RefSeq	NP_102964.1. NC_002678.2.
3D structure databases
HSSP	HSSP built from PDB template 2FDN based on UniProtKB P00198.
ProteinModelPortal	Q98KR4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1225627.
GenomeReviews	Gene locus mll1359 in contig BA000012_GR.
KEGG	mlo:mll1359.
NMPDR	fig|266835.1.peg.1069.
PATRIC	22476368. VBIMesLot2464_1095.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG724359.
OMA	AMKMVTE.
ProtClustDB	PRK05888.
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_RHILO

Accession

Primary (citable) accession number: Q98KR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	October 1, 2001
Last modified:	January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program