Q7DDS1 (NUOI_NEIMB) 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:	NMB0251

Organism

Neisseria meningitidis serogroup B

Taxonomic identifier

491 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	159 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	intracellular Inferred from electronic annotation. Source: InterPro 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 quinone binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 159	159	NADH-quinone oxidoreductase subunit I HAMAP MF_01351		PRO_0000250917
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)
	Q7DDS1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: FA5764DAD0009EE9	FASTA	159	18,156
	10 20 30 40 50 60 MANLVKTFLL GELVKGMGVT LKNFFARKDT IYFPEEKTPQ SVRFRGLHAQ RRYPNGEERC 70 80 90 100 110 120 IACKLCEAVC PAMAINIESE EREDGTRRTK RYDIDLTKCI FCGFCEEACP TDAIVETHIF 130 140 150 EYHGEKKGDL HMTKPILLAI GDKYEAEIAK RKAADAPYR

References

[1]

"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. , Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C. Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58 / Serogroup B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002098 Genomic DNA. Translation: AAF40705.1.
RefSeq	NP_273307.1. NC_003112.2.
3D structure databases
HSSP	HSSP built from PDB template 2FDN based on UniProtKB P00198.
ProteinModelPortal	Q7DDS1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBNEIT00000009015; EBNEIP00000008635; EBNEIG00000009015.
GeneID	902362.
GenomeReviews	Gene locus NMB0251 in contig AE002098_GR.
KEGG	nme:NMB0251.
PATRIC	20355580. VBINeiMen85645_0314.
TIGR	NMB0251.
Phylogenomic databases
GeneTree	EBGT00050000020569.
HOGENOM	HBG724359.
OMA	CPAMAIT.
ProtClustDB	PRK05888.
Enzyme and pathway databases
BioCyc	NMEN122586:NMB_0251-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. IPR015880. Znf_C2H2-like. [Graphical view]
Gene3D	G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit.
KO	K00338.
Pfam	PF12838. Fer4_7. 1 hit. [Graphical view]
SMART	SM00355. ZnF_C2H2. 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_NEIMB

Accession

Primary (citable) accession number: Q7DDS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	July 5, 2004
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