Structural annotation of Rv2753c (dihydrodipicolinate synthase)
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| Structural annotation of Rv2753c (dihydrodipicolinate synthase)
| |
| Name | |
| Dihydrodipicolinate Synthase | |
| Identifiers | |
| Swiss Prot | |
| Genbank | |
| PDB | |
| Chemical data | |
| Formula | ? |
| Mol. wt. | 30,858 Da |
| Pharmacokinetic data | |
| Bioavailability | ? |
| Solubility | ? |
| Isoelectric-Point | 5.57 |
Contents |
General
dapA catalyzes the formation of dihydrodipicolinate from L-aspartate 4-semialdehyde and pyruvate.
L-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + 2H2O.
This protein is eesential for optimal growth of M.tb and found in the cytoplasm as predicted by the WoLFPSORT and Subloc Server. HMMpfam found one domain PF00701 and has Helix Turn Helix secondary structure.
Amino Acid Sequence of Rv2753c
>Rv2753c, TB.seq 3066222:3067121 MW:30827 VTTVGFDVAARLGTLLTAMVTPFSGDGSLDTATAARLANHLVDQGCDGLVVSGTTGESPTTTDGEKIELLRAVLEAVGDR ARVIAGAGTYDTAHSIRLAKACAAEGAHGLLVVTPYYSKPPQRGLQAHFTAVADATELPMLLYDIPGRSAVPIEPDTIRA LASHPNIVGVKDAKADLHSGAQIMADTGLAYYSGDDALNLPWLAMGATGFISVIAHLAAGQLRELLSAFGSGDIATARKI NIAVAPLCNAMSRLGGVTLSKAGLRLQGIDVGDPRLPQVAATPEQIDALAADMRAASVLR
PDB Structure
This protein structure is available in PDB and having code 1XXX
Human Homologue Blast Result
| subject ids | % identity | % positives | alignment length | evalue |
| sp|Q9BXD5 | 28 | 46.33 | 300 | 3.00E-023 |
| sp|Q86XE5 | 26.57 | 46.15 | 286 | 4.00E-022 |
| sp|Q9UG63 | 26.49 | 37.75 | 151 | 0.45 |
| sp|O14556 | 22.09 | 50 | 86 | 2 |
| sp|Q7Z7B0 | 27.69 | 44.62 | 65 | 2.7 |
Antigens
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