NADH-ubiquinone oxidoreductase 75 kDa subunit - Dictyostelium citrinum (Slime mold)

Preferred order of sections

Names and origin

Protein names

Recommended name:
NADH-ubiquinone oxidoreductase 75 kDa subunit
EC=1.6.5.3
EC=1.6.99.3

Alternative name(s):
Complex I-75kD
Short name=CI-75kD

Gene names

Name:	nad11
Synonyms:	ndufs1

Encoded on

Mitochondrion

Organism

Dictyostelium citrinum (Slime mold)

Taxonomic identifier

361072 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	688 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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 about 45 different subunits By similarity.
Subcellular location	Mitochondrion inner membrane By 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. Contains 1 4Fe-4S Mo/W bis-MGD-type domain.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
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: EC electron carrier activity Inferred from electronic annotation. Source: InterPro metal ion 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 – 688

688

NADH-ubiquinone oxidoreductase 75 kDa subunit

PRO_0000327378

Regions

Domain

1 – 85

85

2Fe-2S ferredoxin-type

Domain

223 – 279

57

4Fe-4S Mo/W bis-MGD-type

Sites

Metal binding

38

1

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

49

1

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

52

1

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

66

1

Iron-sulfur 1 (2Fe-2S) By similarity

Metal binding

101

1

Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity

Metal binding

105

1

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

108

1

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

114

1

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

153

1

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

156

1

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

159

1

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

204

1

Iron-sulfur 3 (4Fe-4S) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q2LCP5 [UniParc].

Last modified April 8, 2008. Version 2.
Checksum: FDC7CCB227832A0C
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FASTA

688

79,605

        10         20         30         40         50         60 
MLIRFKINEI ECEVDEEKED LTILQACTAN GIEIPRFCYH EKLTIAGNCR MCLVYVTNEE 

        70         80         90        100        110        120 
KLLAACGIPL DENFDDESIE TEIDEILKAR EGVMEFLLIN HPLDCPICDQ GGECDLQEQT 

       130        140        150        160        170        180 
IAYGLDTGRF YIKKRAVEVK AFGRLIKGIM TRCIHCTRCV RFLTEIAGVN ELGVLGRGYN 

       190        200        210        220        230        240 
MEIGTYKKNV IIESELSGNI IDLCPVGALT SAVYAYKGRP WELKNIKGID IFDTVLTPIN 

       250        260        270        280        290        300 
YQVKGGEIFR ILPRINDRLN EEWITDKVRF HYESYKIIEK MRKDTPSYKI QANKFIELSW 

       310        320        330        340        350        360 
KTALKMVFKV LLNKKNKVDL IIGSKINSTN LRIYKELMNR LGSKNYITEN GLLFKKFNYD 

       370        380        390        400        410        420 
FRENYINSND LYNVDQNDLV LLCGINLRVE SPLLNIKLRN INFGDDEIET RKKIGIIGNK 

       430        440        450        460        470        480 
FDWKQESEYL GSTVNSMLKV FEGRFPYCQQ IKKSKAPLIL VGSSLLSRIA ISLQEIRAAF 

       490        500        510        520        530        540 
EIASNIKPEN VLLITQGANF GMALEEGIFK ENFSKGGNVL YSIDSNEYKV SKTINYIIYQ 

       550        560        570        580        590        600 
GILNDTFENK IDLYLPSKHY FEDFESDREI YVNTFGQRSE IEKLRISKGN KIKENSMIGY 

       610        620        630        640        650        660 
IQLMYLNKKE MNRKEKEQKE IKITYRGIKQ KEKRQVKINK NLTINNIIDN YYMTDINSRL 

       670        680 
SKNLMITGQL RKEKKIMEAG SWKNKTCI

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References

[1]	"Evolutionary trends found in social amoebae." Gloeckner G., Schaap P., Winckler T. Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ336395 Genomic DNA. Translation: ABC60398.4.
RefSeq	YP_003579824.1. NC_007787.2.
3D structure databases
ProteinModelPortal	Q2LCP5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	9086870.
Family and domain databases
Gene3D	3.10.20.30. 1 hit.
InterPro	IPR001041. 2Fe-2S_ferredoxin-type. IPR012675. Beta-grasp_dom. IPR006656. Mopterin_OxRdtase. IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS. IPR010228. NADH_UbQ_OxRdtase_Gsu. IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. [Graphical view]
Pfam	PF00384. Molybdopterin. 2 hits. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
SMART	SM00929. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
SUPFAM	SSF54292. Ferredoxin. 1 hit.
TIGRFAMs	TIGR01973. NuoG. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. 1 hit. PS51669. 4FE4S_MOW_BIS_MGD. 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_DICCI

Accession

Primary (citable) accession number: Q2LCP5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	April 8, 2008
Last modified:	May 29, 2013
This is version 44 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Family and domain databases

Entry information

Relevant documents