Pseudomonas aeruginosa UCBPP-PA14, PA14_09950

Cytoplasmic
Cytoplasmic Membrane
Periplasmic
Outer Membrane
Extracellular
Unknown
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Gene Ontology

Ontology Accession Term GO Evidence Evidence Ontology (ECO) Code Reference Comments
Molecular Function GO:0016491 oxidoreductase activity
ISM
Inferred from Sequence Model
Term mapped from: InterPro:PF07992
ECO:0000259
match to InterPro signature evidence used in automatic assertion

Functional Classifications Manually Assigned by PseudoCAP

Putative enzymes Other UCBPP-PA14 genes in this class

Functional Predictions from Interpro

Analysis Accession Description Interpro Accession Interpro Description Amino Acid Start Amino Acid Stop E-value
PRINTS PR00469 Pyridine nucleotide disulphide reductase class-II signature - - 117 125 3.2E-8
SUPERFAMILY SSF51905 FAD/NAD(P)-binding domain IPR036188 FAD/NAD(P)-binding domain superfamily 129 230 2.07E-5
PRINTS PR00368 FAD-dependent pyridine nucleotide reductase signature - - 116 134 1.6E-12
SUPERFAMILY SSF51905 FAD/NAD(P)-binding domain IPR036188 FAD/NAD(P)-binding domain superfamily 13 305 5.92E-26
Gene3D G3DSA:3.50.50.60 - IPR036188 FAD/NAD(P)-binding domain superfamily 130 237 1.1E-82
Pfam PF07992 Pyridine nucleotide-disulphide oxidoreductase IPR023753 FAD/NAD(P)-binding domain 18 285 5.1E-18
PANTHER PTHR48105 THIOREDOXIN REDUCTASE 1-RELATED-RELATED - - 17 295 2.5E-28
PRINTS PR00469 Pyridine nucleotide disulphide reductase class-II signature - - 19 41 3.2E-8
PRINTS PR00368 FAD-dependent pyridine nucleotide reductase signature - - 261 283 1.6E-12
PRINTS PR00469 Pyridine nucleotide disulphide reductase class-II signature - - 139 151 3.2E-8
PRINTS PR00469 Pyridine nucleotide disulphide reductase class-II signature - - 154 178 3.2E-8
PRINTS PR00368 FAD-dependent pyridine nucleotide reductase signature - - 20 39 1.6E-12
Gene3D G3DSA:3.50.50.60 - IPR036188 FAD/NAD(P)-binding domain superfamily 18 300 1.1E-82

Search for additional functional domains at the NCBI CDD database website. Go to this protein's amino acid sequence and follow the link.