Q2GDY1 (NUOA_NEOSM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
NADH dehydrogenase I subunit A
NDH-1 subunit A
NUO1

Gene names

Name:	nuoA
Ordered Locus Names:	NSE_0429

Organism

Neorickettsia sennetsu (strain Miyayama) [Complete proteome] [HAMAP]

Taxonomic identifier

222891 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Neorickettsia › Ehrlichia sennetsu

Protein attributes

Sequence length	130 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-Rule MF_01394
Catalytic activity	NADH + quinone = NAD+ + quinol. HAMAP-Rule MF_01394
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; Multi-pass membrane protein By similarity HAMAP-Rule MF_01394.
Sequence similarities	Belongs to the complex I subunit 3 family.
Sequence caution	The sequence ABD45956.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transport
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)
Biological_process	photosynthesis, light reaction Inferred from electronic annotation. Source: HAMAP transport Inferred from electronic annotation. Source: UniProtKB-KW
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 sequence or structural similarity. Source: TIGR NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro 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 – 130	130	NADH-quinone oxidoreductase subunit A HAMAP-Rule MF_01394		PRO_0000362705
Regions
	Transmembrane	17 – 37	21	Helical; Potential
	Transmembrane	74 – 94	21	Helical; Potential
	Transmembrane	99 – 119	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q2GDY1 [UniParc]. Last modified February 10, 2009. Version 2. Checksum: B3835B3675DC6972	FASTA	130	14,633
	10 20 30 40 50 60 MLESSVVGIG KWVVEDYIFV GLFFVVACFI SCVMLALPVF IAPSSHERHK GDSYECGFDK 70 80 90 100 110 120 LSSTGERFNV RFYLVGILFI IFDLEIIFLF PWAVSARELG PAAFVSVLIF LIILTVGFVY 130 EFVSGALDWR

References

[1]

"Comparative genomics of emerging human ehrlichiosis agents." Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N. , Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H. PLoS Genet. 2:208-222(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Miyayama.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000237 Genomic DNA. Translation: ABD45956.1. Different initiation.
RefSeq	YP_506315.1. NC_007798.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	222891.NSE_0429.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABD45956; ABD45956; NSE_0429.
GeneID	3932227.
KEGG	nse:NSE_0429.
PATRIC	22680913. VBINeoSen119815_0385.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0838.
HOGENOM	HOG000100119.
KO	K00330.
ProtClustDB	CLSK2527844.
Enzyme and pathway databases
BioCyc	NSEN222891:GHFU-451-MONOMER.
Family and domain databases
HAMAP	MF_01394. NDH1_NuoA.
InterPro	IPR023043. NAD(P)H_OxRDtase_bac/plastid. IPR000440. NADH_UbQ/plastoQ_OxRdtase_su3. [Graphical view]
PANTHER	PTHR11058. PTHR11058. 1 hit.
Pfam	PF00507. Oxidored_q4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUOA_NEOSM

Accession

Primary (citable) accession number: Q2GDY1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program