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Reviewed, UniProtKB/Swiss-Prot Q1R3U7 (STHA_ECOUT)

Last modified February 9, 2010. Version 34. 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: UTI89_C4555
OrganismEscherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier364106 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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_0000260234

Regions

Nucleotide binding36 – 4510FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1R3U7-1 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 2D7405D1E2D062FD

FASTA46651,560
        10         20         30         40         50         60 
MPHSYDYDAI VIGSGPGGEG AAMGLVKQGA RVAVIERYQN VGGGCTHWGT IPSKALRHAV 

        70         80         90        100        110        120 
SRIIEFNQNP LYSDHSRLLR SSFADILNHA DNVINQQTRM RQGFYERNHC EILQGNARFV 

       130        140        150        160        170        180 
DEHTLALDCP DGSVETLTAE KFVIACGSRP YHPTDVDFTH PRIYDSDSIL SMHHEPRHVL 

       190        200        210        220        230        240 
IYGAGVIGCE YASIFRGMDV KVDLINTRDR LLAFLDQEMS DSLSYHFWNS GVVIRHNEEY 

       250        260        270        280        290        300 
EKIEGCDDGV IMHLKSGKKL KADCLLYANG RTGNTDSLAL QNIGLETDSR GQLKVNSMYQ 

       310        320        330        340        350        360 
TAQPHVYAVG DVIGYPSLAS AAYDQGRIAA QALVKGEATA HLIEDIPTGI YTIPEISSVG 

       370        380        390        400        410        420 
KTEQQLTAMK VPYEVGRAQF KHLARAQIVG MNVGTLKILF HRETKEILGI HCFGERAAEI 

       430        440        450        460 
IHIGQAIMEQ KGGGNTIEYF VNTTFNYPTM AEAYRVAALN GLNRLF 

« Hide

References

[1]"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000243 Genomic DNA. Translation: ABE09967.1.
RefSeqYP_543498.1.

3D structure databases

SMRQ1R3U7. Positions 7-464.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1R3U7.

Genome annotation databases

GeneID3993309.
GenomeReviewsGene locus UTI89_C4555 in contig CP000243_GR.
KEGGeci:UTI89_C4555.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1249.
HOGENOMHBG515043.
OMARDIGEPR.

Enzyme and pathway databases

BioCycECOL364106:UTI89_C4555-MONOMER.

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_ECOUT
AccessionPrimary (citable) accession number: Q1R3U7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: May 16, 2006
Last modified: February 9, 2010
This is version 34 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