Reviewed, UniProtKB/Swiss-Prot O84971 (NUOC_RHOCA)

Names and origin

Protein names

Recommended name:
    NADH-quinone oxidoreductase subunit C
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I subunit C
    NDH-1 subunit C

Gene names

Name:

nuoC

Organism

Rhodobacter capsulatus (Rhodopseudomonas capsulata)

Taxonomic identifier

1061 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length	199 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	NADH + quinone = NAD+ + quinol. HAMAP MF_01357
Subunit structure	NDH-1 is composed of 14 different subunits. Subunits nuoB, C, D, E, F, and G constitute the peripheral sector of the complex By similarity.
Subcellular location	Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity.
Sequence similarities	Belongs to the complex I 30 kDa subunit family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cell inner membrane Cell membrane Membrane
Ligand	NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: HAMAP photosynthesis, light reaction Inferred from electronic annotation. Source: HAMAP transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	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 – 199	199	NADH-quinone oxidoreductase subunit C HAMAP MF_01357		PRO_0000118676

Sequences

	Sequence		Length	Mass (Da)
	O84971-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: A5206009EB914C95	FASTA	199	23,090
	10 20 30 40 50 60 MSEKLQDLAA HVAQQRPGDV ISAEVVQGEL TVTVKPEGIA DFVRFLRDDA GCRFTTLVDL 70 80 90 100 110 120 TAVDWPERVE RFEMVWHFLS MWKNQRIRVK AGLAEDAMCP SIVEVYPAAN WYEREVFDMF 130 140 150 160 170 180 GILFSGHPDL RRLLTDYGFR GHPLRKDFPT TGYIELRYDE VQKRVVYEPV KLAQEYRQFD 190 FLSPWEGAQS VLPGDEKRS

References

[1]	Dupuis A., Issartel J.P. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 33303 / B10.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF029365 Genomic DNA. Translation: AAC24987.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.6.99.5. 567.
Family and domain databases
HAMAP	MF_01357. [Tree]
InterPro	IPR010218. NADH_DH_csu. IPR001268. NADH_UbQ_OxRdtase_30kDa_su. [Graphical view]
Pfam	PF00329. Complex1_30kDa. 1 hit. [Graphical view]
ProDom	PD001581. Complex1_30K. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01961. NuoC_fam. 1 hit.
PROSITE	PS00542. COMPLEX1_30K. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUOC_RHOCA

Accession

Primary (citable) accession number: O84971

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1998
Last modified:	June 16, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)