B3I5S2 (B3I5S2_ECOLX) Unreviewed, UniProtKB/TrEMBL
Last modified
January 25, 2012.
Version 26.
History...
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Soluble pyridine nucleotide transhydrogenase HAMAP MF_00247 Short name=STH HAMAP MF_00247 EC=1.6.1.1 HAMAP MF_00247 Alternative name(s): NAD(P)(+) transhydrogenase [B-specific] HAMAP MF_00247 | ||||||
| Gene names |
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| Organism | Escherichia coli E22 EMBL EDV83021.1 | ||||||
| Taxonomic identifier | 340185 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 466 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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 SAAS SAAS004099 |
| Catalytic activity | NADPH + NAD+ = NADP+ + NADH. HAMAP MF_00247 SAAS SAAS004099 |
| Cofactor | Binds 1 FAD per subunit By similarity. HAMAP MF_00247 SAAS SAAS004099 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00247. |
| Sequence similarities | Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. HAMAP MF_00247 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm HAMAP MF_00247 SAAS SAAS004099 |
| Ligand | FAD HAMAP MF_00247 SAAS SAAS022962 Flavoprotein HAMAP MF_00247 SAAS SAAS004099 NAD HAMAP MF_00247 SAAS SAAS004099 NADP HAMAP MF_00247 SAAS SAAS004099 |
| Molecular function | Oxidoreductase HAMAP MF_00247 SAAS SAAS004099 EMBL EDV83021.1 |
| Gene Ontology (GO) | |
| Biological process | NADP metabolic process Inferred from electronic annotation. Source: HAMAP cell redox homeostasisInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | NAD(P)+ transhydrogenase (B-specific) activity Inferred from electronic annotation. Source: HAMAP flavin adenine dinucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequences
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References
| [1] | Rasko D.A., Rosovitz M.J., Kaper J.B., Boedecker E.C., Myers G.S.A., Seshadri R., Cer R.Z., Jiang L., Ravel J. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: E22 EMBL EDV83021.1. |
| [2] | Rasko D., Rosovitz M., Myers G., Seshadri R., Cer R., Jiang L., Ravel J., Fricke W.F., Sebastian Y. Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: E22 EMBL EDV83021.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AAJV02000012 Genomic DNA. Translation: EDV83021.1. |
3D structure databases | |
| ProteinModelPortal | B3I5S2. |
| SMR | B3I5S2. Positions 5-464. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| PATRIC | 26540822. VBIEscCol79205_2371. |
Family and domain databases | |
| HAMAP | MF_00247. SthA. [Tree] |
| InterPro | IPR016156. 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] |
| 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. |
| SUPFAM | SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | B3I5S2_ECOLX | ||||||||
| Accession | Primary (citable) accession number: B3I5S2 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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