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P0A1Y5 (NUOG_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:STY2553, t0541
OrganismSalmonella typhi [Complete proteome] [HAMAP]
Taxonomic identifier90370 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length908 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 By similarity.

Sequence similarities

Belongs to the complex I 75 kDa subunit family.

Contains 1 2Fe-2S ferredoxin-type domain.

Sequence caution

The sequence AAO68247.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAD07555.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 908907NADH-quinone oxidoreductase subunit G
PRO_0000118553

Regions

Domain2 – 83822Fe-2S ferredoxin-type

Sites

Metal binding341Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding451Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding481Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding671Iron-sulfur 1 (2Fe-2S) By similarity
Metal binding991Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
Metal binding1031Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1061Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1121Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1511Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1541Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding1571Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2011Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2281Iron-sulfur 4 (4Fe-4S) By similarity
Metal binding2311Iron-sulfur 4 (4Fe-4S) By similarity
Metal binding2351Iron-sulfur 4 (4Fe-4S) By similarity
Metal binding2631Iron-sulfur 4 (4Fe-4S) By similarity

Experimental info

Sequence conflict8591S → F in AAO68247. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P0A1Y5 [UniParc].

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

FASTA908100,028
        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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL627274 Genomic DNA. Translation: CAD07555.1. Different initiation.
AE014613 Genomic DNA. Translation: AAO68247.1. Different initiation.
PIRAI0796.

3D structure databases

ProteinModelPortalP0A1Y5.
ModBaseSearch...

Proteomic databases

PRIDEP0A1Y5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GenomeReviewsGene locus t0541 in contig AE014613_GR.
Gene locus STY2553 in contig AL513382_GR.
KEGGstt:t0541.
sty:STY2553.
PATRIC18543070. VBISalEnt120419_2583.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG488172.
OMAPSICHGC.
ProtClustDBPRK08166.

Enzyme and pathway databases

BioCycSENT209261:T0541-MONOMER.
SENT220341:STY2553-MONOMER.

Family and domain databases

InterProIPR009010. Asp_de-COase-like_fold.
IPR012675. Beta-grasp_ferredoxin-type.
IPR001041. Ferredoxin.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_Fe4S4_dom.
IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
IPR010228. NADH_UbQ_OxRdtase_Gsu.
IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
[Graphical view]
Gene3DG3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
KOK00336.
PfamPF00111. 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]
SMARTSM00926. Molybdop_Fe4S4. 1 hit.
SM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMSSF50692. Asp_decarb_fold. 1 hit.
SSF54292. Ferredoxin. 1 hit.
TIGRFAMsTIGR01973. NuoG. 1 hit.
PROSITEPS00197. 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]
ProtoNetSearch...

Entry information

Entry nameNUOG_SALTI
AccessionPrimary (citable) accession number: P0A1Y5
Secondary accession number(s): P33900
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families