Reviewed, UniProtKB/Swiss-Prot Q4QSC5 (NQO9_RHOMR)

Names and origin

Protein names

Recommended name:
    NADH-quinone oxidoreductase subunit 9
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I subunit 9
    NDH-1 subunit 9

Gene names

Name:

nqo9

Organism

Rhodothermus marinus (Rhodothermus obamensis)

Taxonomic identifier

29549 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Sphingobacteria › Sphingobacteriales › Rhodothermaceae › Rhodothermus

Protein attributes

Sequence length	230 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 menaquinone. 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 NQO7-14 constitute the membrane sector of the complex By similarity. HAMAP MF_01351
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
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
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
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 iron ion binding Inferred from electronic annotation. Source: HAMAP 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 – 230	230	NADH-quinone oxidoreductase subunit 9 HAMAP MF_01351		PRO_0000245739
Regions
	Domain	60 – 93	34	4Fe-4S ferredoxin-type 1
	Domain	104 – 133	30	4Fe-4S ferredoxin-type 2
Sites
	Metal binding	73	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	76	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	79	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	83	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	113	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	116	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	119	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	123	1	Iron-sulfur 1 (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4QSC5-1 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: E951770E49179E57	FASTA	230	27,120
	10 20 30 40 50 60 MPGKPVNLAS PNERKLNFWE RLYLPAVVQG LAYTWRKMRS PRYTFQYPDE LWYPPDSYRG 70 80 90 100 110 120 RPVLVEENGR PRCVACGLCA RACPPLAISM QAKEVDDVKE REPAWFEINM LRCIYCGYCE 130 140 150 160 170 180 EVCPEEAIVM SKEYDLTFQS RDEAIFGLEK LLVPAERLKD RLEWLDRYKD PQYGQHWEFR 190 200 210 220 230 KENNLHSLKD RPFLKWLLEE EGMEELKSTH LRPEEPVAAE RSWGGVRAEG

References

[1]

"A nhaD Na+/H+ antiporter and a pcd homologues are among the Rhodothermus marinus complex I genes." Melo A.M.P., Lobo S.A.L., Sousa F.L., Fernandes A.S., Pereira M.M., Hreggvidsson G.O., Kristjansson J.K., Saraiva L.M., Teixeira M. Biochim. Biophys. Acta 1709:95-103(2005) [PubMed: 16023073] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PRQ 62B.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY972099 Genomic DNA. Translation: AAY42993.1.
3D structure databases
SMR	Q4QSC5. Positions 47-157.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.6.99.5. 1132.
Family and domain databases
HAMAP	MF_01351. NDH1_NuoI. [Tree]
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR009051. Helical_ferredxn. IPR010226. NADH_quinone_OxRdtase_chainI. [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

NQO9_RHOMR

Accession

Primary (citable) accession number: Q4QSC5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	July 19, 2005
Last modified:	February 9, 2010
This is version 37 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)