NADH-quinone oxidoreductase subunit G - Salmonella typhimurium

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Reviewed, UniProtKB/Swiss-Prot P0A1Y4 (NUOG_SALTY)

Last modified June 16, 2009. Version 34. History...

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

Gene names

Name:	nuoG
Ordered Locus Names:	STM2323

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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Protein attributes

Sequence length	908 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Subunit structure	Composed of 13 different subunits. Subunits nuoCD, E, F, and G constitute the peripheral sector of the complex.
Sequence similarities	Belongs to the complex I 75 kDa subunit family. Contains 1 2Fe-2S ferredoxin-type domain.
Sequence caution	The sequence L42521 differs from that shown. Reason: Frameshift at positions 715 and 806.

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Ontologies

Keywords
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome
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

Initiator methionine

Removed By similarity

Chain

2 – 908

907

NADH-quinone oxidoreductase subunit G

PRO_0000118554

Regions

Domain

2 – 83

2Fe-2S ferredoxin-type

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

103

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

Metal binding

106

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

Metal binding

112

Iron-sulfur 2 (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

157

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

Metal binding

201

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

Metal binding

228

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

Metal binding

231

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

Metal binding

235

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

Metal binding

263

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

Experimental info

Sequence conflict

678

A → V Ref.3

Sequence conflict

786

I → L Ref.3

Sequence conflict

847

A → T Ref.3

Sequence conflict

854

A → T Ref.3

Sequence conflict

888

M → I Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A1Y4-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6A4BAB18E60C20EC
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FASTA

908

100,028

        10         20         30         40         50         60 
MATIHVDGKE YEVNGADNLL QACLSLGLDI PYFCWHPALG SVGACRQCAV KQYQNAEDTR 

        70         80         90        100        110        120 
GRLVMSCMTP ATDGTFISID DEEAKQFRES VVEWLMTNHP HDCPVCEEGG NCHLQDMTVM 

       130        140        150        160        170        180 
TGHSFRRYRF TKRTHRNQDL GPFISHEMNR CIACYRCVRY YKDYADGTDL GVYGAHDNVY 

       190        200        210        220        230        240 
FGRPEDGTLE SEFSGNLVEI CPTGVFTDKT HSERYNRKWD MQFAPSICQQ CSIGCNISPG 

       250        260        270        280        290        300 
ERYGELRRIE NRYNGTVNHY FLCDRGRFGY GYVNLKDRPR QPVQRRGDDF ITLNAEQAMQ 

       310        320        330        340        350        360 
GAADILRQSK KVIGIGSPRA SIESNFALRE LVGAENFYTG IARGEQERLQ LALKVLREGG 

       370        380        390        400        410        420 
IYTPALREIE SYDAVLVLGE DVTQTGARVA LAVRQAVKGK AREMAAAQKV ADWQIAAILN 

       430        440        450        460        470        480 
IGQRAKHPLF VTNVDDTRLD DIAAWTYRAP VEDQARLGFA IAHALDNTAP AVDGIDSDLQ 

       490        500        510        520        530        540 
NKIDVIVQAL AGAKKPLIIS GTNAGSSEVI QAAANVAKAL KGRGADVGIT MIARSVNSMG 

       550        560        570        580        590        600 
LGMMGGGSLD DALGELETGS ADAVVVLEND LHRHASATRV NAALAKAPLV MVVDHQRTAI 

       610        620        630        640        650        660 
MENAHLVLSA ASFAESDGTV INNEGRAQRF FQVYDPAYYD NKTIMLESWR WLHSLHSTVE 

       670        680        690        700        710        720 
NREVDWTQLD HVIDAVIAAM PQFAGIKDAA PDATFRIRGQ KLAREPHRYS GRTAMRANIS 

       730        740        750        760        770        780 
VHEPRQPQDK DTMFAFSMEG NNQPTAPRSE IPFAWAPGWN SPQAWNKFQD EVGGKLRHGD 

       790        800        810        820        830        840 
PGVRLIEATE GGLDYFTTVP ASFQAQDGQW RIAPYYHLFG SDELSQRSPV FQSRMPQPYI 

       850        860        870        880        890        900 
KLNPADAAKL GVNAGTRVSF SYDGNTVTLP VEISEGLAAG QVGLPMGMPG IAPVLAGARL 


EDLREAQQ

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[2]	"Mutants defective in the energy-conserving NADH dehydrogenase of Salmonella typhimurium identified by a decrease in energy-dependent proteolysis after carbon starvation." Archer C.D., Wang X., Elliott T. Proc. Natl. Acad. Sci. U.S.A. 90:9877-9881(1993) [PubMed: 8234329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-612.
[3]	"Influence of genes encoding proton-translocating enzymes on suppression of Salmonella typhimurium growth and colonization." Zhang-Barber L.Z., Turner A.K., Martin G., Fraenkel G., Dougan G., Barrow P.A. J. Bacteriol. 179:7186-7190(1997) [PubMed: 9371470] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 612-908. Strain: F98.

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Cross-references

Sequence databases
	AE008804 Genomic DNA. Translation: AAL21224.1. Different initiation. L22504 Unassigned DNA. Translation: AAA16063.1. Different initiation. L42521 Genomic DNA. No translation available.
RefSeq	NP_461265.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1253845.
GenomeReviews	Gene locus STM2323 in contig AE006468_GR.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P0A1Y4.
OMA	P0A1Y4. EVGGHLR.
Enzyme and pathway databases
BioCyc	STYP99287:STM2323-MON.
BRENDA	1.6.99.5. 2.
Family and domain databases
InterPro	IPR006058. 2Fe2S_fd_BS. 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. IPR010228. NADH_UbQ_OxRdtase_Gsu. 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. PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 1 hit. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR01973. NuoG. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. False negative. 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...

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Entry information

Entry name

NUOG_SALTY

Accession

Primary (citable) accession number: P0A1Y4
Secondary accession number(s): P33900

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 34 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