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Reviewed, UniProtKB/Swiss-Prot Q66G61 (STHA_YERPS)

Last modified February 9, 2010. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Soluble pyridine nucleotide transhydrogenase
      Short name=STH
    EC=1.6.1.1
Alternative name(s):
    NAD(P)(+) transhydrogenase [B-specific]
Gene names
Name: sthA
Synonyms: udhA
Ordered Locus Names: YPTB0121
OrganismYersinia pseudotuberculosis [Complete proteome] [HAMAP]
Taxonomic identifier633 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation By similarity. HAMAP MF_00247

Catalytic activity

NADPH + NAD+ = NADP+ + NADH. HAMAP MF_00247

Cofactor

Binds 1 FAD per subunit By similarity. HAMAP MF_00247

Subcellular location

Cytoplasm By similarity HAMAP MF_00247.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
NAD
NADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processNADP metabolic process

Inferred from electronic annotation. Source: HAMAP

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

NAD(P)+ transhydrogenase (B-specific) activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Soluble pyridine nucleotide transhydrogenase HAMAP MF_00247
PRO_0000260248

Regions

Nucleotide binding36 – 4510FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q66G61-1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: D6CD965D6CF3E2CE

FASTA46651,382
        10         20         30         40         50         60 
MQQHFHFDAI VIGSGPGGEG AAMGLVKQGA RVAVIERYNN VGGGCTHWGT IPSKALRHAV 

        70         80         90        100        110        120 
SRIIEFNQNP LYSDNARTIK SSFADILNHA DRVINQQTRM RQGFYDRNHC HMFSGDASFI 

       130        140        150        160        170        180 
DANTVNVRYA DGTSDTLQAD NIVIATGSRP YRPVNVDFNH ERIYDSDTIL QLSHEPQHVI 

       190        200        210        220        230        240 
IYGAGVIGCE YASIFRGLSV KVDLINTRDR LLAFLDQEMS DALSYHFWNN GVVIRHNEEF 

       250        260        270        280        290        300 
EQIEGTTDGV IVHLKSGKKV KADCLLYANG RTGNTSGLGL ENIGLEADSR GLLKVNSMYQ 

       310        320        330        340        350        360 
TALSHVYAVG DVIGYPSLAS AAYDQGRIAA QAMIKGEANV HLIEDIPTGI YTIPEISSVG 

       370        380        390        400        410        420 
KTEQELTAMK VPYEVGRAQF KHLARAQIVG MDTGSLKILF HRETKQILGI HCFGERAAEI 

       430        440        450        460 
IHIGQAIMEQ KGEGNTLEYF VNTTFNYPTM AEAYRVAALN GLNRLF 

« Hide

References

[1]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed: 15358858] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953 / Serotype I.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX936398 Genomic DNA. Translation: CAH19361.1.
RefSeqYP_068670.1.

3D structure databases

HSSPHSSP built from PDB template 2F5Z based on UniProtKB P09622.
SMRQ66G61. Positions 7-464.
ModBaseSearch...

Genome annotation databases

GeneID2956644.
GenomeReviewsGene locus YPTB0121 in contig BX936398_GR.
KEGGyps:YPTB0121.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG515043.
OMARDIGEPR.

Enzyme and pathway databases

BioCycYPSE273123:YPTB0121-MONOMER.
BRENDA1.6.1.1. 20871.

Family and domain databases

HAMAPMF_00247. SthA.
[Tree]
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000815. Hg_reductase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
PR00945. HGRDTASE.
ProtoNetSearch...

Entry information

Entry nameSTHA_YERPS
AccessionPrimary (citable) accession number: Q66G61
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: October 11, 2004
Last modified: February 9, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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