Q0TFG4 (NUOH_ECOL5) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	nuoH
Ordered Locus Names:	ECP_2321

Organism

Escherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

362663 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	325 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. This subunit may bind ubiquinone By similarity. HAMAP-Rule MF_01350
Catalytic activity	NADH + quinone = NAD+ + quinol. HAMAP-Rule MF_01350
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 inner membrane; Multi-pass membrane protein Potential HAMAP-Rule MF_01350.
Sequence similarities	Belongs to the complex I subunit 1 family.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome
Gene Ontology (GO)
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	NADH dehydrogenase (quinone) activity Inferred from electronic annotation. Source: EC 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 – 325	325	NADH-quinone oxidoreductase subunit H HAMAP-Rule MF_01350		PRO_0000298811
Regions
	Transmembrane	11 – 31	21	Helical; Potential
	Transmembrane	81 – 101	21	Helical; Potential
	Transmembrane	114 – 134	21	Helical; Potential
	Transmembrane	154 – 174	21	Helical; Potential
	Transmembrane	186 – 206	21	Helical; Potential
	Transmembrane	237 – 257	21	Helical; Potential
	Transmembrane	265 – 285	21	Helical; Potential
	Transmembrane	304 – 324	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q0TFG4 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 954F54BD8E1617A9	FASTA	325	36,205
	10 20 30 40 50 60 MSWISPELIE ILLTVLKAVV ILLVVVTCGA FMSFGERRLL GLFQNRYGPN RVGWGGSLQL 70 80 90 100 110 120 VADMIKMFFK EDWIPKFSDR VIFTLAPMIA FTSLLLAFAI VPVSPGWVVA DLNIGILFFL 130 140 150 160 170 180 MMAGLAVYAV LFAGWSSNNK YSLLGAMRAS AQTLSYEVFL GLSLMGVVAQ AGSFNMTDIV 190 200 210 220 230 240 NSQAHVWNVI PQFFGFITFA IAGVAVCHRH PFDQPEAEQE LADGYHIEYS GMKFGLFFVG 250 260 270 280 290 300 EYIGIVTISA LMVTLFFGGW QGPLLPPFIW FALKTAFFMM MFILIRASLP RPRYDQVMSF 310 320 GWKICLPLTL INLLVTAAVI LWQAQ

References

[1]

"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536." Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J. Mol. Microbiol. 61:584-595(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 536 / UPEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000247 Genomic DNA. Translation: ABG70315.1.
RefSeq	YP_670216.1. NC_008253.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	362663.ECP_2321.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABG70315; ABG70315; ECP_2321.
GeneID	4191457.
KEGG	ecp:ECP_2321.
PATRIC	18195411. VBIEscCol77757_2349.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1005.
HOGENOM	HOG000228276.
KO	K00337.
OMA	VGEYINI.
PhylomeDB	Q0TFG4.
ProtClustDB	PRK06076.
Enzyme and pathway databases
BioCyc	ECOL362663:GIY5-2333-MONOMER.
Family and domain databases
HAMAP	MF_01350. NDH1_NuoH.
InterPro	IPR001694. NADH_UbQ_OxRdtase_su1/FPO. IPR018086. NADH_UbQ_OxRdtase_su1_CS. [Graphical view]
PANTHER	PTHR11432. PTHR11432. 1 hit.
Pfam	PF00146. NADHdh. 1 hit. [Graphical view]
PROSITE	PS00667. COMPLEX1_ND1_1. 1 hit. PS00668. COMPLEX1_ND1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUOH_ECOL5

Accession

Primary (citable) accession number: Q0TFG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 21, 2007
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program