Q9ZDH5 (NUOE_RICPR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NADH-quinone oxidoreductase subunit E
EC=1.6.99.5

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

Gene names

Name:	nuoE
Ordered Locus Names:	RP353

Organism

Rickettsia prowazekii (strain Madrid E)

Taxonomic identifier

272947 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group

Protein attributes

Sequence length	177 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. 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.
Catalytic activity	NADH + quinone = NAD+ + quinol.
Cofactor	Binds 1 2Fe-2S cluster Potential.
Sequence similarities	Belongs to the complex I 24 kDa subunit family.

Ontologies

Keywords
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding NAD
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NAD binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase (quinone) activity Inferred from electronic annotation. Source: EC 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 – 177	177	NADH-quinone oxidoreductase subunit E		PRO_0000118701
Sites
	Metal binding	93	1	Iron-sulfur (2Fe-2S) Potential
	Metal binding	98	1	Iron-sulfur (2Fe-2S) Potential
	Metal binding	134	1	Iron-sulfur (2Fe-2S) Potential
	Metal binding	138	1	Iron-sulfur (2Fe-2S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9ZDH5 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 5CE2C81C67F3A9E6	FASTA	177	20,462
	10 20 30 40 50 60 MNTKITNFTF AFDKKNLNLA ETIIKKYPPE GKRSAILPLL DLAQRQNGGW LHVSAIEYVA 70 80 90 100 110 120 NMLEMPYMRA YEVATFYTMF NLNPIGKYHI QVCTTTPCWL RGSDNIMKIC EKKLAIKHKE 130 140 150 160 170 TTKDQKFTLS EIECLGACVN APVVQINDDY YEDLNEAKME KLIEQYLNEF KSKMQNG

References

[1]

"The genome sequence of Rickettsia prowazekii and the origin of mitochondria." Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G. Nature 396:133-140(1998) [PubMed: 9823893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Madrid E.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ235271 Genomic DNA. Translation: CAA14813.1.
PIR	C71692.
RefSeq	NP_220737.1. NC_000963.1.
3D structure databases
ProteinModelPortal	Q9ZDH5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	883409.
GenomeReviews	Gene locus RP353 in contig AJ235269_GR.
KEGG	rpr:RP353.
PATRIC	17901475. VBIRicPro72556_0363.
Phylogenomic databases
HOGENOM	HBG616790.
OMA	AMNYIAD.
ProtClustDB	PRK07539.
Enzyme and pathway databases
BioCyc	RPRO272947:RP353-MONOMER.
Family and domain databases
InterPro	IPR002023. NADH_UbQ_OxRdtase_24kDa_su. IPR012336. Thioredoxin-like_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K00334.
PANTHER	PTHR10371. Cmplx1_24kDa. 1 hit.
Pfam	PF01257. Complex1_24kDa. 1 hit. [Graphical view]
PIRSF	PIRSF000216. NADH_DH_24kDa. 1 hit.
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
TIGRFAMs	TIGR01958. NuoE_fam. 1 hit.
PROSITE	PS01099. COMPLEX1_24K. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUOE_RICPR

Accession

Primary (citable) accession number: Q9ZDH5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program