NADH-quinone oxidoreductase subunit G 2

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Reviewed, UniProtKB/Swiss-Prot P56914 (NUOG2_RHIME)

Last modified June 16, 2009. Version 75. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    NADH-quinone oxidoreductase subunit G 2
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I subunit G 2
    NDH-1 subunit G 2

Gene names

Name:	nuoG2
Ordered Locus Names:	RA0828
ORF Names:	SMa1523

Encoded on

Plasmid pSymA (megaplasmid 1)

Organism

Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP]

Taxonomic identifier

382 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

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Protein attributes

Sequence length	853 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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.
Cofactor	Binds 1 2Fe-2S cluster per subunit By similarity. Binds 3 4Fe-4S clusters per subunit By similarity.
Sequence similarities	Belongs to the complex I 75 kDa subunit family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 2 4Fe-4S ferredoxin-type domains.

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Ontologies

Keywords
Domain	Repeat
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome Plasmid
Gene Ontology (GO)
Biological process	ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro
Cellular component	membrane Inferred from electronic annotation. Source: InterPro
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 molybdenum ion binding Inferred from electronic annotation. Source: InterPro quinone binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 853

853

NADH-quinone oxidoreductase subunit G 2

PRO_0000118560

Regions

Domain

1 – 78

2Fe-2S ferredoxin-type

Domain

139 – 170

4Fe-4S ferredoxin-type 1

Domain

179 – 209

4Fe-4S ferredoxin-type 2

Sites

Metal binding

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

Metal binding

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

Metal binding

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

Metal binding

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

Metal binding

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

Metal binding

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

Metal binding

101

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

Metal binding

107

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

Metal binding

148

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

Metal binding

151

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

Metal binding

154

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

Metal binding

198

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

Metal binding

224

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

227

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

231

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

259

Iron-sulfur 4 (4Fe-4S) Potential

Experimental info

Sequence conflict

211

K → R in CAB51635. Ref.1

Sequence conflict

285

T → A in CAB51635. Ref.1

Sequence conflict

452

F → L in CAB51635. Ref.1

Sequence conflict

459

T → I in CAB51635. Ref.1

Sequence conflict

544

S → G in CAB51635. Ref.1

Sequence conflict

554

R → K in CAB51635. Ref.1

Sequence conflict

679

R → Q in CAB51635. Ref.1

Sequence conflict

734

A → G in CAB51635. Ref.1

Sequence conflict

756

H → R in CAB51635. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P56914-1 [UniParc].

Last modified November 2, 2001. Version 2.
Checksum: CDF867CE3BD11A0B
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FASTA

853

93,346

        10         20         30         40         50         60 
MIKVTIDEQS LEVEAGSTVL AAAERLGIEI PTFCYWKRLP PLASCRMCLV EIEGLRRLQP 

        70         80         90        100        110        120 
ACATVAADGM VVRTNTPLIE ETRSSMLDML LANHPLDCPI CDKGGECELQ DMVMAYGPGE 

       130        140        150        160        170        180 
SRFRDPKRVF HSKDIRLSPV IIMNVNRCIQ CQRCVRMCEE VVGAVALGTV EKGMDTAVTG 

       190        200        210        220        230        240 
FEGSLASCDQ CGNCVEVCPV GALMSFPYRY KARPWDLAET DTICPHCGTG CQLTVGARKG 

       250        260        270        280        290        300 
EFMRVRSDWE HGVNRETLCV RGRFGLDFIE SRDRIKRPMI RRDGTLTPVS WEEAGDFLRQ 

       310        320        330        340        350        360 
RLGVAEGKAA GGLISPRLPN EVLYQFQKLM RTVLRTNNVD CSSRWSAPLD ILVPIVASFY 

       370        380        390        400        410        420 
SRDPLEQVIG KDCVLIIGGN VTEENPVTEY LLRDAARRRH TRLLMLSARP SRLDADARAV 

       430        440        450        460        470        480 
LRAHPGGEGQ SLAAVVAALV AVTDEGLPDD IFAKTSGTTA SSGANDALDR LVSTLKEGRS 

       490        500        510        520        530        540 
VTLLVSVDLL RSPLARKTLE QLGNLLQLLR LLGKEPSLQF LFDRANQMGA WDMGVLPGVL 

       550        560        570        580        590        600 
PGLSPIADEA TRTRFERSWG AEIPREPGAD VDAMLELCEK GGMGVLYVVG SDPLISYPDR 

       610        620        630        640        650        660 
EFVERALGAA NLLIVQDAFL TDTAGLADVV LPAAGYGEES GTFTNNEGRT QALRKFREPA 

       670        680        690        700        710        720 
FDARSNLAIF GFIAALRERP LQPSTETVIF EEMTRLVPAY EGLTWEGLGA DGAFTTSAPK 

       730        740        750        760        770        780 
PWTSGFFAPL SAPAVTDVLQ LITGNCLFHN GYVSEHSETL NSVADDPFIE MSAQDAAGLS 

       790        800        810        820        830        840 
LSDGDQVLVR SARGELTAKL KVNRRFPHGL VFVPENYRAL RLNSLMRRGE YPCPVEIREC 

       850 
AKRAASALDE ERV

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Rhizobium meliloti carries two sets of nuo genes." Putnoky P., Jady B., Chellapilla K.P., Barta F., Kiss E. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 41.
[2]	"Nucleotide sequence and predicted functions of the entire Sinorhizobium meliloti pSymA megaplasmid." Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H. Long S.R. Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001) [PubMed: 11481432] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021.

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Cross-references

Sequence databases
	AJ245399 Genomic DNA. Translation: CAB51635.1. AE006469 Genomic DNA. Translation: AAK65486.1.
PIR	D95365.
RefSeq	NP_436074.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1235864.
GenomeReviews	Gene locus RA0828 in contig AE006469_GR.
KEGG	sme:SMa1523.
NMPDR	fig\|266834.1.peg.828.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P56914.
OMA	P56914. KGGECEL.
Enzyme and pathway databases
BioCyc	SMEL266834:SMA1523-MON.
BRENDA	1.6.99.5. 142.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. IPR017896. 4Fe4S_Fe-S-bd. IPR001450. 4Fe4S_Fe_S_bd_subgr. IPR017900. 4Fe4S_Fe_S_CS. IPR009010. Asp_de-COase-like_fold. IPR001041. Ferredoxin. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4. IPR006657. MPT_dinuc_bd. IPR000283. NADH_UbQ_OxRdtase_75KDa_su_CS. IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. [Graphical view]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
Pfam	PF00111. Fer2. 1 hit. PF00037. Fer4. 1 hit. PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 2 hits. PF01568. Molydop_binding. 1 hit. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
PROSITE	PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. 1 hit. PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 2 hits. PS00641. COMPLEX1_75K_1. 1 hit. PS00642. COMPLEX1_75K_2. 1 hit. PS00643. COMPLEX1_75K_3. 1 hit. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

NUOG2_RHIME

Accession

Primary (citable) accession number: P56914

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 2, 2001
Last modified:	June 16, 2009
This is version 75 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents