Reviewed, UniProtKB/Swiss-Prot Q0MQG3 (NDUS2_PONAB)

Names and origin

Protein names

Recommended name:
    NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial
    EC=1.6.5.3
    EC=1.6.99.3
Alternative name(s):
    NADH-ubiquinone oxidoreductase 49 kDa subunit
    Complex I-49kD
      Short name=CI-49kD

Gene names

Name:

NDUFS2

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	463 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.
Catalytic activity	NADH + ubiquinone = NAD+ + ubiquinol. NADH + acceptor = NAD+ + reduced acceptor.
Cofactor	Binds 1 4Fe-4S cluster.
Subunit structure	Complex I is composed of 45 different subunits. Component of the iron-sulfur (IP) fragment of the enzyme By similarity.
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Matrix side By similarity.
Sequence similarities	Belongs to the complex I 49 kDa subunit family.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW response to oxidative stress Inferred from sequence or structural similarity. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial respiratory chain complex I Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NAD or NADH binding Inferred from electronic annotation. Source: InterPro NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinone binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 33	33	Mitochondrion By similarity
	Chain	34 – 463	430	NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial		PRO_0000251858
Sites
	Metal binding	326	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	332	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	347	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q0MQG3-1 [UniParc]. Last modified September 19, 2006. Version 1. Checksum: 67898E268A31A5B6	FASTA	463	52,528
	10 20 30 40 50 60 MAALRALGGL RGVAAQVLRP GAGVRLPIQP SRGVRQWQPD VEWAQQFGGA VMYPSKETAH 70 80 90 100 110 120 WKPPPWNDVE PPKDTIVKNM TLNFGPQHPA AHGVLRLVME LSGEMVRKCD PHIGLLHRGT 130 140 150 160 170 180 EKLIEYKTYL QALPYFDRLD YVSMMCNEQA YSLAVEKLLN IRPPPRAQWI RVLFGEITRL 190 200 210 220 230 240 LNHIMAVTTH ALDLGAMTPF FWLFEEREKM FEFYERVSGA RMHAAYIRPG GVHQDLPLGL 250 260 270 280 290 300 MDDIYQFSKN FSLRLDELEE LLTNNRIWRN RTIDIGVVTA EEALNYGFSG VMLRGSGIQW 310 320 330 340 350 360 DLRKTQPYDV YDQVEFDVPV GSRGDCYDRY LCRVEEMRQS LRIIAQCLNK MPPGEIKVDD 370 380 390 400 410 420 AKVSPPKRAE MKTSMESLIH HFKLYTEGYQ VPPGATYTAI EAPKGEFGVY LVSDGSSRPY 430 440 450 460 RCKIKAPGFA HLASLDKMSK GHMLADVVAI IGTQDIVFGE VDR

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	DQ885671 mRNA. Translation: ABH12180.1.
3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q0MQG3.
OMA	Q0MQG3. MYEAVSG.
Enzyme and pathway databases
BRENDA	1.6.5.3. 269192. 1.6.99.3. 269192.
Family and domain databases
InterPro	IPR010219. NADH_DH_1_dsu. IPR001135. NADH_Q_OxRdtase_suD. IPR014029. NADH_UbQ_OxRdtase_su-49kDa_CS. [Graphical view]
Pfam	PF00346. Complex1_49kDa. 1 hit. [Graphical view]
TIGRFAMs	TIGR01962. NuoD. 1 hit.
PROSITE	PS00535. COMPLEX1_49K. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NDUS2_PONAB

Accession

Primary (citable) accession number: Q0MQG3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	September 19, 2006
Last modified:	June 16, 2009
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)