Skip Header

Contribute Send feedback
Read comments (?) or add your own

B1JQ50 (STHA_YERPY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:YPK_4078
OrganismYersinia pseudotuberculosis serotype O:3 (strain YPIII) [Complete proteome] [HAMAP]
Taxonomic identifier502800 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

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 processcell redox homeostasis

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD(P)+ transhydrogenase (B-specific) activity

Inferred from electronic annotation. Source: EC

flavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Soluble pyridine nucleotide transhydrogenase HAMAP MF_00247
PRO_1000100865

Regions

Nucleotide binding36 – 4510FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
B1JQ50 [UniParc].

Last modified April 29, 2008. 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]"Complete sequence of Yersinia pseudotuberculosis YPIII."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YPIII.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000950 Genomic DNA. Translation: ACA70337.1.
RefSeqYP_001722790.1. NC_010465.1.

3D structure databases

ProteinModelPortalB1JQ50.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1JQ50.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6091072.
GenomeReviewsGene locus YPK_4078 in contig CP000950_GR.
KEGGypy:YPK_4078.
PATRIC18665949. VBIYerPse127545_4404.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG515043.
OMAGEGNTIE.
ProtClustDBPRK05249.

Family and domain databases

HAMAPMF_00247. SthA.
[Tree]
InterProIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR022962. STH.
[Graphical view]
Gene3DG3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
KOK00322.
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. FAD/NAD-linked_reductase_dimer. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSTHA_YERPY
AccessionPrimary (citable) accession number: B1JQ50
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: January 25, 2012
This is version 33 of the entry and version 1 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents