Reviewed,
UniProtKB/Swiss-Prot P57112 (STHA_PSEAE)
Last modified
November 25, 2008.
Version 63.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Soluble pyridine nucleotide transhydrogenase Short name=STH EC=1.6.1.1 Alternative name(s): NAD(P)(+) transhydrogenase [B-specific] | ||||||
| Gene names |
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| Organism | Pseudomonas aeruginosa [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 287 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 464 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
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. |
| Catalytic activity | NADPH + NAD(+) = NADP(+) + NADH. |
| Cofactor | Binds 1 FAD per subunit. |
| Enzyme regulation | Strongly activated by NADPH and 2'-AMP and inhibited by NADP(+). Ca(2+) increases the activation and decreases the inhibition effect. |
| Subunit structure | Homooligomer; probably composed of four stacked rings of 7 or 8 monomers. Forms filamentous structures. |
| Subcellular location | CytoplasmBy similarity. |
| Sequence similarities | Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | FAD Flavoprotein NAD NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | NADP metabolic process Inferred from electronic annotation. Source: HAMAP cell redox homeostasisInferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: HAMAP |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro NAD(P)+ transhydrogenase (B-specific) activityInferred from electronic annotation. Source: HAMAP electron carrier activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. Olson M.V.Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228. |
| [2] | "Pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa: purification by affinity chromatography and physicochemical properties." Wermuth B., Kaplan N.O. Arch. Biochem. Biophys. 176:136-143(1976) [PubMed: 823872] [Abstract] Cited for: CHARACTERIZATION. |
| [3] | "Pseudomonas aeruginosa transhydrogenase: affinity of substrates for the regulatory site and possible hysteretic behavior." Widmer F., Kaplan N.O. Biochem. Biophys. Res. Commun. 76:1287-1292(1977) [PubMed: 20086] [Abstract] Cited for: CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| AE004091 Genomic DNA. Translation: AAG06379.1. | |
| PIR | H83271. |
| RefSeq | NP_251681.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1EBD based on UniProtKB P11959. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 878679. |
| GenomeReviews | Gene locus PA2991 in contig AE004091_GR. |
| KEGG | pae:PA2991. |
Organism-specific databases | |
| PseudoCAP | PA2991. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P57112. |
Enzyme and pathway databases | |
| BioCyc | PAER208964:PA2991-MON. |
Family and domain databases | |
| HAMAP | MF_00247. [Tree] |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR000815. Hg_reductase. IPR001100. Pyr_nuc-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view] |
| Gene3D | G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit. |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. PR00945. HGRDTASE. PR00411. PNDRDTASEI. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| ProtoNet | Search... |
Entry information
| Entry name | STHA_PSEAE | ||||||||
| Accession | Primary (citable) accession number: P57112 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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