Reviewed, UniProtKB/Swiss-Prot Q0MQG1 (NDUS1_GORGO)

Names and origin

Protein names

Recommended name:
    NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
    EC=1.6.5.3
    EC=1.6.99.3
Alternative name(s):
    Complex I-75kD
      Short name=CI-75kD

Gene names

Name:

NDUFS1

Organism

Gorilla gorilla gorilla (Lowland gorilla)

Taxonomic identifier

9595 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Gorilla

Protein attributes

Sequence length	727 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone By similarity. This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized By similarity.
Catalytic activity	NADH + ubiquinone = NAD(+) + ubiquinol. NADH + acceptor = NAD(+) + reduced acceptor.
Cofactor	Binds 1 2Fe-2S cluster per subunit By similarity. Binds 2 4Fe-4S clusters per subunit By similarity.
Subunit structure	Complex I is composed of 45 different subunits By similarity.
Subcellular location	Mitochondrion inner membraneBy similarity. Note= Matrix and cytoplasmic side of the mitochondrial inner membrane By similarity.
Sequence similarities	Belongs to the complex I 75 kDa subunit family. Contains 1 2Fe-2S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Acetylation
Gene Ontology (GO)
Biological process	ATP metabolic process Inferred from sequence or structural similarity. Source: UniProtKB ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro apoptosis Inferred from sequence or structural similarity. Source: UniProtKB cellular respiration Inferred from sequence or structural similarity. Source: UniProtKB oxygen and reactive oxygen species metabolic process Inferred from sequence or structural similarity. Source: UniProtKB regulation of mitochondrial membrane potential Inferred from sequence or structural similarity. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial intermembrane space Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial respiratory chain complex I Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 23	23	Mitochondrion By similarity
	Chain	24 – 727	704	NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial		PRO_0000251853
Regions
	Domain	30 – 108	79	2Fe-2S ferredoxin-type
Sites
	Metal binding	64	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	75	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	78	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	92	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	124	1	Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
	Metal binding	128	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	131	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	137	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	176	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	179	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	182	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	226	1	Iron-sulfur 3 (4Fe-4S) By similarity
Amino acid modifications
	Modified residue	84	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0MQG1-1 [UniParc]. Last modified September 19, 2006. Version 1. Checksum: 860FE5560CB47D3C	FASTA	727	79,450
	10 20 30 40 50 60 MLRIPVRKAL VGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI 70 80 90 100 110 120 PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW NILTNSEKSK KAREGVMEFL 130 140 150 160 170 180 LANHPLDCPI CDQGGECDLQ DQSMMFGNDR SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT 190 200 210 220 230 240 RCIRFASEIA GVDDLGTTGR GNDMQVGTYI EKMFMSELSG NIIDICPVGA LTSKPYAFTA 250 260 270 280 290 300 RPWETRKTES IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEXWISDKT RFAYDGLKRQ 310 320 330 340 350 360 RLTEPMVRNE KGLLTYTSWE DALSRVAGML QSFQGKDVAA IAGGLVDAEA LVALKDLLNR 370 380 390 400 410 420 VDSDTLCTEE VFPTAGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARIRK 430 440 450 460 470 480 SWLHNDLKVA LIGSPVDLTY TYDHLGDSPK ILQDIASGSH PFSQVLKEAK KPMVVLGSSA 490 500 510 520 530 540 LQRNDGAAIL AAVSSIAQKI RMTSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIRKN 550 560 570 580 590 600 PPKVLFLLGA DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE 610 620 630 640 650 660 GRAQQTKVAV TPPGLAREDW KIIRALSEIA GMTLPYDTLD QVRNRLEEVS PNLVRYDDIE 670 680 690 700 710 720 GANYFQQANE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA VEEPSIC

References

[1]	"Adaptive selection of mitochondrial complex I subunits during primate radiation." Mishmar D., Ruiz-Pesini E., Mondragon-Palomino M., Procaccio V., Gaut B., Wallace D.C. Gene 378:11-18(2006) [PubMed: 16828987] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ885673 mRNA. Translation: ABH12182.1.
3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q0MQG1.
Family and domain databases
InterPro	IPR001041. Ferredoxin. IPR006656. Mopterin_OxRdtase. IPR000283. NADH_DHase_75KDa_su_CS. IPR010228. NADH_quinone_OxRdtase_G. IPR015405. NuoG_C. [Graphical view]
Pfam	PF09326. DUF1982. 1 hit. PF00111. Fer2. 1 hit. PF00384. Molybdopterin. 1 hit. [Graphical view]
TIGRFAMs	TIGR01973. NuoG. 1 hit.
PROSITE	PS51085. 2FE2S_FER_2. 1 hit. PS00641. COMPLEX1_75K_1. 1 hit. PS00642. COMPLEX1_75K_2. 1 hit. PS00643. COMPLEX1_75K_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NDUS1_GORGO

Accession

Primary (citable) accession number: Q0MQG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	September 19, 2006
Last modified:	November 25, 2008
This is version 19 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)