Protein Info for MPMX20_02149 in Enterobacter sp. TBS_079

Annotation: 3-hydroxyadipyl-CoA dehydrogenase

These analyses and tools can help you predict a protein's function, but be skeptical. For enzymes, over 10% of annotations from KEGG or SEED are probably incorrect. For other types of proteins, the error rates may be much higher. MetaCyc and Swiss-Prot have low error rates, but the best hits in these databases are often quite distant, so this protein's function may not be the same. TIGRFam has low error rates. Finally, many experimentally-characterized proteins are not in any of these databases. To find relevant papers, use PaperBLAST.

Protein Families and Features

• TIGR02279: 3-hydroxyacyl-CoA dehydrogenase PaaC
  • amino acids 3 to 474 (472 residues), 759.5 bits, E=9.1e-233
• PF03446: NAD_binding_2
  • amino acids 7 to 71 (65 residues), 23.7 bits, E=9e-09
• PF02737: 3HCDH_N
  • amino acids 7 to 184 (178 residues), 217.6 bits, E=2.5e-68
• PF00725: 3HCDH
  • amino acids 188 to 285 (98 residues), 103.4 bits, E=1.6e-33
  • amino acids 389 to 466 (78 residues), 57.2 bits, E=4.1e-19
• PF18321: 3HCDH_RFF
  • amino acids 324 to 386 (63 residues), 37.4 bits, E=5.6e-13

Best Hits

Swiss-Prot: 80% identical to PAAH_ECOLI: 3-hydroxyadipyl-CoA dehydrogenase (paaH) from Escherichia coli (strain K12)

KEGG orthology group: K00074, 3-hydroxybutyryl-CoA dehydrogenase [EC: 1.1.1.157] (inferred from 91% identity to enc:ECL_02146)

MetaCyc: 80% identical to 3-hydroxyadipyl-CoA dehydrogenase (Escherichia coli K-12 substr. MG1655)
3-hydroxyacyl-CoA dehydrogenase. [EC: 1.1.1.35]

Predicted SEED Role

"3-hydroxyacyl-CoA dehydrogenase PaaC (EC 1.1.1.-)" (EC 1.1.1.-)

MetaCyc Pathways

• oleate β-oxidation (32/35 steps found)
• superpathway of phenylethylamine degradation (11/11 steps found)
• phenylacetate degradation I (aerobic) (9/9 steps found)
• adipate degradation (5/5 steps found)
• fatty acid β-oxidation I (generic) (6/7 steps found)
• superpathway of glyoxylate cycle and fatty acid degradation (11/14 steps found)
• benzoyl-CoA biosynthesis (3/3 steps found)
• fatty acid salvage (5/6 steps found)
• glycerol degradation to butanol (12/16 steps found)
• (R)- and (S)-3-hydroxybutanoate biosynthesis (engineered) (4/5 steps found)
• adipate biosynthesis (4/5 steps found)
• photosynthetic 3-hydroxybutanoate biosynthesis (engineered) (19/26 steps found)
• pyruvate fermentation to hexanol (engineered) (8/11 steps found)
• pyruvate fermentation to butanol II (engineered) (4/6 steps found)
• 1-butanol autotrophic biosynthesis (engineered) (19/27 steps found)
• superpathway of Clostridium acetobutylicum acidogenic fermentation (6/9 steps found)
• fatty acid β-oxidation II (plant peroxisome) (3/5 steps found)
• glutaryl-CoA degradation (3/5 steps found)
• pyruvate fermentation to butanoate (4/7 steps found)
• 2-methyl-branched fatty acid β-oxidation (9/14 steps found)
• methyl ketone biosynthesis (engineered) (3/6 steps found)
• valproate β-oxidation (5/9 steps found)
• 4-hydroxybenzoate biosynthesis III (plants) (2/5 steps found)
• pyruvate fermentation to butanol I (4/8 steps found)
• benzoyl-CoA degradation I (aerobic) (3/7 steps found)
• fatty acid β-oxidation VI (mammalian peroxisome) (3/7 steps found)
• benzoate biosynthesis I (CoA-dependent, β-oxidative) (4/9 steps found)
• 3-phenylpropanoate degradation (4/10 steps found)
• L-glutamate degradation V (via hydroxyglutarate) (4/10 steps found)
• superpathway of Clostridium acetobutylicum solventogenic fermentation (6/13 steps found)
• L-glutamate degradation VII (to butanoate) (5/12 steps found)
• 2-methylpropene degradation (2/8 steps found)
• 3-hydroxypropanoate/4-hydroxybutanate cycle (9/18 steps found)
• superpathway of Clostridium acetobutylicum acidogenic and solventogenic fermentation (8/17 steps found)
• methyl tert-butyl ether degradation (2/10 steps found)
• L-tryptophan degradation III (eukaryotic) (3/15 steps found)
• crotonate fermentation (to acetate and cyclohexane carboxylate) (3/16 steps found)
• benzoate fermentation (to acetate and cyclohexane carboxylate) (3/17 steps found)
• toluene degradation VI (anaerobic) (3/18 steps found)
• cholesterol degradation to androstenedione I (cholesterol oxidase) (2/17 steps found)
• androstenedione degradation I (aerobic) (6/25 steps found)
• platensimycin biosynthesis (6/26 steps found)
• cholesterol degradation to androstenedione II (cholesterol dehydrogenase) (2/22 steps found)
• superpathway of testosterone and androsterone degradation (6/28 steps found)
• androstenedione degradation II (anaerobic) (4/27 steps found)
• superpathway of cholesterol degradation I (cholesterol oxidase) (8/42 steps found)
• superpathway of cholesterol degradation II (cholesterol dehydrogenase) (8/47 steps found)
• superpathway of cholesterol degradation III (oxidase) (4/49 steps found)

KEGG Metabolic Maps

• Alkaloid biosynthesis I
• Aminosugars metabolism
• Ascorbate and aldarate metabolism
• Benzoate degradation via CoA ligation
• Bile acid biosynthesis
• Biosynthesis of alkaloids derived from shikimate pathway
• Biosynthesis of plant hormones
• Biosynthesis of type II polyketide products
• Biosynthesis of unsaturated fatty acids
• Bisphenol A degradation
• Butanoate metabolism
• C21-Steroid hormone metabolism
• Caprolactam degradation
• Fatty acid elongation in mitochondria
• Fatty acid metabolism
• Fructose and mannose metabolism
• Geraniol degradation
• Glycine, serine and threonine metabolism
• Insect hormone biosynthesis
• Linoleic acid metabolism
• Lysine degradation
• Nucleotide sugars metabolism
• Polyketide sugar unit biosynthesis
• Retinol metabolism
• Tetrachloroethene degradation
• Tryptophan metabolism
• Valine, leucine and isoleucine degradation

Isozymes

Compare fitness of predicted isozymes for: 1.1.1.-, 1.1.1.35

Use Curated BLAST to search for 1.1.1.- or 1.1.1.157 or 1.1.1.35

Protein Sequence (475 amino acids)

>MPMX20_02149 3-hydroxyadipyl-CoA dehydrogenase (Enterobacter sp. TBS_079)
MAITVRTVAVIGSGTMGAGIAEVAASHGHQVLMYDIASDAISRAIDGIRQRLASRVTRGK
LSADAGSQILARLLPVTDIEALAAADLVIEAASERIDVKKALFAQLAQICPPQTLLTSNT
SSISVTAIAADVHHPERVAGLHFFNPAPVMKLVEVVSGLATSPEVADALCELALNWGKQP
VRCQSTPGFIVNRVARPFYSEAWRALEEQVAAPEVIDAALRDGGGFPMGPLELTDMIGQD
VNFAVTCSVFNAFWQERRFLPSLVQQELVLAGRLGKKSGKGVYDWHGEIPAVPWLDAVND
SFTPMRVQRRGDGVTEIDELLLIETQGETAQALARRFNCPVVVIDRIERDVAVIAAASDN
PHTATQKAVWYLQQQGHRVLRIADYPGLLVWRTVAMIANEALDALQKGVASEKDIDTAMR
LGVNYPNGPIAWGERLGWQRLLTLLENLQRHYGEERYRPCSLLRQRALLESSYES